Transistors, the building blocks of modern electronics, are typically made of silicon. Because it’s a semiconductor, this material can control the flow of electricity in a circuit. But silicon has fundamental physical limits that restrict how compact and energy-efficient a transistor can be.

MIT researchers have now replaced silicon with a magnetic semiconductor, creating a magnetic transistor that could enable smaller, faster, and more energy-efficient circuits. The material’s magnetism strongly influences its electronic behavior, leading to more efficient control of the flow of electricity. 

The team used a novel magnetic material and an optimization process that reduces the material’s defects, which boosts the transistor’s performance.

The material’s unique magnetic properties also allow for transistors with built-in memory, which would simplify circuit design and unlock new applications for high-performance electronics.

“People have known about magnets for thousands of years, but there are very limited ways to incorporate magnetism into electronics. We have shown a new way to efficiently utilize magnetism that opens up a lot of possibilities for future applications and research,” says Chung-Tao Chou, an MIT graduate student in the departments of Electrical Engineering and Computer Science (EECS) and Physics, and co-lead author of a paper on this advance.

Chou is joined on the paper by co-lead author Eugene Park, a graduate student in the Department of Materials Science and Engineering (DMSE); Julian Klein, a DMSE research scientist; Josep Ingla-Aynes, a postdoc in the MIT Plasma Science and Fusion Center; Jagadeesh S. Moodera, a senior research scientist in the Department of Physics; and senior authors Frances Ross, TDK Professor in DMSE; and Luqiao Liu, an associate professor in EECS, and a member of the Research Laboratory of Electronics; as well as others at the University of Chemistry and Technology in Prague. The paper appears today in Physical Review Letters.

Overcoming the limits

In an electronic device, silicon semiconductor transistors act like tiny light switches that turn a circuit on and off, or amplify weak signals in a communication system. They do this using a small input voltage.

But a fundamental physical limit of silicon semiconductors prevents a transistor from operating below a certain voltage, which hinders its energy efficiency.

To make more efficient electronics, researchers have spent decades working toward magnetic transistors that utilize electron spin to control the flow of electricity. Electron spin is a fundamental property that enables electrons to behave like tiny magnets.

So far, scientists have mostly been limited to using certain magnetic materials. These lack the favorable electronic properties of semiconductors, constraining device performance.

“In this work, we combine magnetism and semiconductor physics to realize useful spintronic devices,” Liu says.

The researchers replace the silicon in the surface layer of a transistor with chromium sulfur bromide, a two-dimensional material that acts as a magnetic semiconductor.

Due to the material’s structure, researchers can switch between two magnetic states very cleanly. This makes it ideal for use in a transistor that smoothly switches between “on” and “off.”

“One of the biggest challenges we faced was finding the right material. We tried many other materials that didn’t work,” Chou says.

They discovered that changing these magnetic states modifies the material’s electronic properties, enabling low-energy operation. And unlike many other 2D materials, chromium sulfur bromide remains stable in air.

To make a transistor, the researchers pattern electrodes onto a silicon substrate, then carefully align and transfer the 2D material on top. They use tape to pick up a tiny piece of material, only a few tens of nanometers thick, and place it onto the substrate.

“A lot of researchers will use solvents or glue to do the transfer, but transistors require a very clean surface. We eliminate all those risks by simplifying this step,” Chou says.

Leveraging magnetism

This lack of contamination enables their device to outperform existing magnetic transistors. Most others can only create a weak magnetic effect, changing the flow of current by a few percent or less. Their new transistor can switch or amplify the electric current by a factor of 10.

They use an external magnetic field to change the magnetic state of the material, switching the transistor using significantly less energy than would usually be required.

The material also allows them to control the magnetic states with electric current. This is important because engineers cannot apply magnetic fields to individual transistors in an electronic device. They need to control each one electrically.

The material’s magnetic properties could also enable transistors with built-in memory, simplifying the design of logic or memory circuits.

A typical memory device has a magnetic cell to store information and a transistor to read it out. Their method can combine both into one magnetic transistor.

“Now, not only are transistors turning on and off, they are also remembering information. And because we can switch the transistor with greater magnitude, the signal is much stronger so we can read out the information faster, and in a much more reliable way,” Liu says.

Building on this demonstration, the researchers plan to further study the use of electrical current to control the device. They are also working to make their method scalable so they can fabricate arrays of transistors.

This research was supported, in part, by the Semiconductor Research Corporation, the U.S. Defense Advanced Research Projects Agency (DARPA), the U.S. National Science Foundation (NSF), the U.S. Department of Energy, the U.S. Army Research Office, and the Czech Ministry of Education, Youth, and Sports. The work was partially carried out at the MIT.nano facilities.

Dangerously unchecked surveillance and rights violations have been a throughline of the Department of Homeland Security since the agency’s creation in the wake of the September 11th attacks. In particular, Immigration and Customs Enforcement (ICE) and Customs and Border Protection (CBP) have been responsible for countless civil liberties and digital rights violations since that time. In the past year, however, ICE and CBP have descended into utter lawlessness, repeatedly refusing to exercise or submit to the democratic accountability required by the Constitution and our system of laws.  

The Trump Administration has made indiscriminate immigration enforcement and mass deportation a key feature of its agenda, with little to no accountability for illegal actions by agents and agency officials. Over the past year, we’ve seen massive ICE raids in cities from Los Angeles to Chicago to Minneapolis. Supercharged by an unprecedented funding increase, immigration enforcement agents haven’t been limited to boots on the ground: they’ve been scanning faces, tracking neighborhood cell phone activity, and amassing surveillance tools to monitor immigrants and U.S. citizens alike. 

The latest enforcement actions in Minnesota have led to federal immigration agents killing Renee Good and Alex Pretti. Both were engaged in their First Amendment right to observe and record law enforcement when they were killed. And it’s only because others similarly exercised their right to record that these killings were documented and widely exposed, countering false narratives the Trump Administration promoted in an attempt to justify the unjustifiable.  

These constitutional violations are systemic, not one-offs. Just last week, the Associated Press reported a leaked ICE memo that authorizes agents to enter homes solely based on “administrative” warrants—lacking any judicial involvement. This government policy is contrary to the “very core” of the Fourth Amendment, which protects us against unreasonable search and seizure, especially in our own homes.  

These violations must stop now. ICE and CBP have grown so disdainful of the rule of law that reforms or guardrails cannot suffice. We join with many others in saying that Congress must vote to reject any further funding of ICE and CBP this week. But that is not enough. It’s time for Congress to do the real work of rebuilding our immigration enforcement system from the ground up, so that it respects human rights (including digital rights) and human dignity, with real accountability for individual officers, their leadership, and the agency as a whole.  

It became the 11th state to file a lawsuit against the petroleum industry, despite efforts by the Trump administration to block the case.

But FEMA protections are now in limbo, with Democrats vowing to block a Homeland Security funding bill after a federal agent killed a Minneapolis protester Saturday.

This is coming:

The Irish government is planning to bolster its police’s ability to intercept communications, including encrypted messages, and provide a legal basis for spyware use.

Employment losses across the clean energy sector undercut the Trump administration's broader push to revive U.S. manufacturing.

State attorneys general warned that six administration actions being challenged in federal court "severely and unlawfully" hinder wind and solar project development.

Last year's "Clear Horizons Act" died in committee after some Democrats warned about its impact on low-income residents.

“Apps don’t understand the details of why snow, sleet or freezing rain happens," a meteorology professor said.

The only way to achieve anything in the semiautonomous Danish territory is through icebreakers’ crucial ability to cut trails through frozen seas.

Climate change has amplified fire conditions in South America and elsewhere, and the recent fires broke out amid a severe heat wave, with high temperatures in some places around 100 degrees Fahrenheit.

South Africa’s electricity minister said the money offered under the compact wasn’t “competitive” with debt available through capital markets.

Nature Climate Change, Published online: 26 January 2026; doi:10.1038/s41558-025-02547-z

Climate change is tightening its grip on the world’s drinking water, threatening both safety and supply. Without urgent and coordinated adaptation of treatment systems, this overlooked vulnerability could compromise global water security.

On his desk, Bryan Bryson ’07, PhD ’13 still has the notes he used for the talk he gave at MIT when he interviewed for a faculty position in biological engineering. On that sheet, he outlined the main question he wanted to address in his lab: How do immune cells kill bacteria?

Since starting his lab in 2018, Bryson has continued to pursue that question, which he sees as critical for finding new ways to target infectious diseases that have plagued humanity for centuries, especially tuberculosis. To make significant progress against TB, researchers need to understand how immune cells respond to the disease, he says.

“Here is a pathogen that has probably killed more people in human history than any other pathogen, so you want to learn how to kill it,” says Bryson, now an associate professor at MIT. “That has really been the core of our scientific mission since I started my lab. How does the immune system see this bacterium and how does the immune system kill the bacterium? If we can unlock that, then we can unlock new therapies and unlock new vaccines.”

The only TB vaccine now available, the BCG vaccine, is a weakened version of a bacterium that causes TB in cows. This vaccine is widely administered in some parts of the world, but it poorly protects adults against pulmonary TB. Although some treatments are available, tuberculosis still kills more than a million people every year.

“To me, making a better TB vaccine comes down to a question of measurement, and so we have really tried to tackle that problem head-on. The mission of my lab is to develop new measurement modalities and concepts that can help us accelerate a better TB vaccine,” says Bryson, who is also a member of the Ragon Institute of Mass General Brigham, MIT, and Harvard.

From engineering to immunology

Engineering has deep roots in Bryson’s family: His great-grandfather was an engineer who worked on the Panama Canal, and his grandmother loved to build things and would likely have become an engineer if she had had the educational opportunity, Bryson says.

The oldest of four sons, Bryson was raised primarily by his mother and grandparents, who encouraged his interest in science. When he was three years old, his family moved from Worcester, Massachusetts, to Miami, Florida, where he began tinkering with engineering himself, building robots out of Styrofoam cups and light bulbs. After moving to Houston, Texas, at the beginning of seventh grade, Bryson joined his school’s math team.

As a high school student, Bryson had his heart set on studying biomedical engineering in college. However, MIT, one of his top choices, didn’t have a biomedical engineering program, and biological engineering wasn’t yet offered as an undergraduate major. After he was accepted to MIT, his family urged him to attend and then figure out what he would study.

Throughout his first year, Bryson deliberated over his decision, with electrical engineering and computer science (EECS) and aeronautics and astronautics both leading contenders. As he recalls, he thought he might study aero/astro with a minor in biomedical engineering and work on spacesuit design.

However, during an internship the summer after his first year, his mentor gave him a valuable piece of advice: “You should study something that will let you have a lot of options, because you don’t know how the world is going to change.”

When he came back to MIT for his sophomore year, Bryson switched his major to mechanical engineering, with a bioengineering track. He also started looking for undergraduate research positions. A poster in the hallway grabbed his attention, and he ended up with working with the professor whose work was featured: Linda Griffith, a professor of biological engineering and mechanical engineering.

Bryson’s experience in the lab “changed the trajectory of my life,” he says. There, he worked on building microfluidic devices that could be used to grow liver tissue from hepatocytes. He enjoyed the engineering aspects of the project, but he realized that he also wanted to learn more about the cells and why they behaved the way they did. He ended up staying at MIT to earn a PhD in biological engineering, working with Forest White.

In White’s lab, Bryson studied cell signaling processes and how they are altered in diseases such as cancer and diabetes. While doing his PhD research, he also became interested in studying infectious diseases. After earning his degree, he went to work with a professor of immunology at the Harvard School of Public Health, Sarah Fortune.

Fortune studies tuberculosis, and in her lab, Bryson began investigating how Mycobacterium tuberculosis interacts with host cells. During that time, Fortune instilled in him a desire to seek solutions to tuberculosis that could be transformative — not just identifying a new antibiotic, for example, but finding a way to dramatically reduce the incidence of the disease. This, he thought, could be done by vaccination, and in order to do that, he needed to understand how immune cells response to the disease. 

“That postdoc really taught me how to think bravely about what you could do if you were not limited by the measurements you could make today,” Bryson says. “What are the problems we really need to solve? There are so many things you could think about with TB, but what’s the thing that’s going to change history?”

Pursuing vaccine targets

Since joining the MIT faculty eight years ago, Bryson and his students have developed new ways to answer the question he posed in his faculty interviews: How does the immune system kill bacteria?

One key step in this process is that immune cells must be able to recognize bacterial proteins that are displayed on the surfaces of infected cells. Mycobacterium tuberculosis produces more than 4,000 proteins, but only a small subset of those end up displayed by infected cells. Those proteins would likely make the best candidates for a new TB vaccine, Bryson says.

Bryson’s lab has developed ways to identify those proteins, and so far, their studies have revealed that many of the TB antigens displayed to the immune system belong to a class of proteins known as type 7 secretion system substrates. Mycobacterium tuberculosis expresses about 100 of these proteins, but which of these 100 are displayed by infected cells varies from person to person, depending on their genetic background.

By studying blood samples from people of different genetic backgrounds, Bryson’s lab has identified the TB proteins displayed by infected cells in about 50 percent of the human population. He is now working on the remaining 50 percent and believes that once those studies are finished, he’ll have a very good idea of which proteins could be used to make a TB vaccine that would work for nearly everyone.

Once those proteins are chosen, his team can work on designing the vaccine and then testing it in animals, with hopes of being ready for clinical trials in about six years.

In spite of the challenges ahead, Bryson remains optimistic about the possibility of success, and credits his mother for instilling a positive attitude in him while he was growing up.

“My mom decided to raise all four of her children by herself, and she made it look so flawless,” Bryson says. “She instilled a sense of ‘you can do what you want to do,’ and a sense of optimism. There are so many ways that you can say that something will fail, but why don’t we look to find the reasons to continue?”

One of the things he loves about MIT is that he has found a similar can-do attitude across the Institute.

“The engineer ethos of MIT is that yes, this is possible, and what we’re trying to find is the way to make this possible,” he says. “I think engineering and infectious disease go really hand-in-hand, because engineers love a problem, and tuberculosis is a really hard problem.”

When not tackling hard problems, Bryson likes to lighten things up with ice cream study breaks at Simmons Hall, where he is an associate head of house. Using an ice cream machine he has had since 2009, Bryson makes gallons of ice cream for dorm residents several times a year. Nontraditional flavors such as passion fruit or jalapeno strawberry have proven especially popular.

“Recently I did flavors of fall, so I did a cinnamon ice cream, I did a pear sorbet,” he says. “Toasted marshmallow was a huge hit, but that really destroyed my kitchen.”

We're taking part in Copyright Week, a series of actions and discussions supporting key principles that should guide copyright policy. Every day this week, various groups are taking on different elements of copyright law and policy, and addressing what's at stake, and what we need to do to make sure that copyright promotes creativity and innovation.

Long before generative AI, copyright holders warned that new technologies for reading and analyzing information would destroy creativity. Internet search engines, they argued, were infringement machines—tools that copied copyrighted works at scale without permission. As they had with earlier information technologies like the photocopier and the VCR, copyright owners sued.

Courts disagreed. They recognized that copying works in order to understand, index, and locate information is a classic fair use—and a necessary condition for a free and open internet.

Today, the same argument is being recycled against AI. It’s whether copyright owners should be allowed to control how others analyze, reuse, and build on existing works.

Fair Use Protects Analysis—Even When It’s Automated

U.S. courts have long recognized that copying for purposes of analysis, indexing, and learning is a classic fair use. That principle didn’t originate with artificial intelligence. It doesn’t disappear just because the processes are performed by a machine.

Copying that works in order to understand them, extract information from them, or make them searchable is transformative and lawful. That’s why search engines can index the web, libraries can make digital indexes, and researchers can analyze large collections of text and data without negotiating licenses from millions of rightsholders. These uses don’t substitute for the original works; they enable new forms of knowledge and expression.

Training AI models fits squarely within that tradition. An AI system learns by analyzing patterns across many works. The purpose of that copying is not to reproduce or replace the original texts, but to extract statistical relationships that allow the AI system to generate new outputs. That is the hallmark of a transformative use. 

Attacking AI training on copyright grounds misunderstands what’s at stake. If copyright law is expanded to require permission for analyzing or learning from existing works, the damage won’t be limited to generative AI tools. It could threaten long-standing practices in machine learning and text-and-data mining that underpin research in science, medicine, and technology. 

Researchers already rely on fair use to analyze massive datasets such as scientific literature. Requiring licenses for these uses would often be impractical or impossible, and it would advantage only the largest companies with the money to negotiate blanket deals. Fair use exists to prevent copyright from becoming a barrier to understanding the world. The law has protected learning before. It should continue to do so now, even when that learning is automated. 

A Road Forward For AI Training And Fair Use 

One court has already shown how these cases should be analyzed. In Bartz v. Anthropic, the court found that using copyrighted works to train an AI model is a highly transformative use. Training is a kind of studying how language works—not about reproducing or supplanting the original books. Any harm to the market for the original works was speculative. 

The court in Bartz rejected the idea that an AI model might infringe because, in some abstract sense, its output competes with existing works. While EFF disagrees with other parts of the decision, the court’s ruling on AI training and fair use offers a good approach. Courts should focus on whether training is transformative and non-substitutive, not on fear-based speculation about how a new tool could affect someone’s market share. 

AI Can Create Problems, But Expanding Copyright Is the Wrong Fix 

Workers’ concerns about automation and displacement are real and should not be ignored. But copyright is the wrong tool to address them. Managing economic transitions and protecting workers during turbulent times may be core functions of government, but copyright law doesn’t help with that task in the slightest. Expanding copyright control over learning and analysis won’t stop new forms of worker automation—it never has. But it will distort copyright law and undermine free expression. 

Broad licensing mandates may also do harm by entrenching the current biggest incumbent companies. Only the largest tech firms can afford to negotiate massive licensing deals covering millions of works. Smaller developers, research teams, nonprofits, and open-source projects will all get locked out. Copyright expansion won’t restrain Big Tech—it will give it a new advantage.  

Fair Use Still Matters

Learning from prior work is foundational to free expression. Rightsholders cannot be allowed to control it. Courts have rejected that move before, and they should do so again.

Search, indexing, and analysis didn’t destroy creativity. Nor did the photocopier, nor the VCR. They expanded speech, access to knowledge, and participation in culture. Artificial intelligence raises hard new questions, but fair use remains the right starting point for thinking about training.

Spock befriends a giant space squid in the comic Star Trek: Strange New Worlds: The Seeds of Salvation #5.

As usual, you can also use this squid post to talk about the security stories in the news that I haven’t covered.

Blog moderation policy.

Pablo Jarillo-Herrero, the Cecil and Ida Green Professor of Physics at MIT, has won the 2025 BBVA Foundation Frontiers of Knowledge Award in Basic Sciences for “discoveries concerning the ‘magic angle’ that allows the behavior of new materials to be transformed and controlled.”

He shares the 400,000-euro award with Allan MacDonald of the University of Texas at Austin. According to the BBVA Foundation, “the pioneering work of the two physicists has achieved both the theoretical foundation and experimental validation of a new field where superconductivity, magnetism, and other properties can be obtained by rotating new two-dimensional materials like graphene.” Graphene is a single layer of carbon atoms arranged in hexagons resembling a honeycomb structure.

Theoretical foundation, experimental validation

In a theoretical model published in 2011, MacDonald predicted that on twisting two graphene layers at a given angle, of around 1 degree, the interaction of electrons would produce new emerging properties.
 
In 2018, Jarillo-Herrero delivered the experimental confirmation of this “magic angle” by rotating two graphene sheets in a way that transformed the material’s behavior, giving rise to new properties like superconductivity.

The physicists’ work “has opened up new frontiers in physics by demonstrating that rotating matter to a given angle allows us to control its behavior, obtaining properties that could have a major industrial impact,” explained award committee member María José García Borge, a research professor at the Institute for the Structure of Matter. “Superconductivity, for example, could bring about far more sustainable electricity transmission, with virtually no energy loss.”

Almost science fiction

MacDonald’s initial discovery had little immediate impact. It was not until some years later, when it was confirmed in the laboratory by Jarillo-Herrero, that its true importance was revealed. 

“The community would never have been so interested in my subject, if there hadn’t been an experimental program that realized that original vision,” observes MacDonald, who refers to his co-laureate’s achievement as “almost science fiction.”

Jarillo-Herrero had been intrigued by the possible effects of placing two graphene sheets on top of each other with a precise rotational alignment, because “it was uncharted territory, beyond the reach of the physics of the past, so was bound to produce some interesting results.”

But the scientist was still unsure of how to make it work in the lab. For years, he had been stacking together layers of the super-thin material, but without being able to specify the angle between them. Finally, he devised a way to do so, making the angle smaller and smaller until he got to the “magic” angle of 1.1 degrees at which the graphene revealed some extraordinary behavior.

“It was a big surprise, because the technique we used, though conceptually straightforward, was hard to pull off in the lab,” says Jarillo-Herrero, who is also affiliated with the Materials Research Laboratory.

Since 2009, the BBVA has given Frontiers of Knowledge Awards to more than a dozen MIT faculty members. The Frontiers of Knowledge Awards, spanning eight prize categories, recognize world-class research and cultural creation and aim to celebrate and promote the value of knowledge as a global public good. The BBVA Foundation works to support scientific research and cultural creation, disseminate knowledge and culture, and recognize talent and innovation. 

Researchers in Class of 1942 Professor of Chemistry Matthew D. Shoulders’ lab have uncovered a sinister hidden mechanism that can allow cancer cells to survive (and, in some cases, thrive) even when hit with powerful drugs. The secret lies in a cellular “safety net” that gives cancer the freedom to develop aggressive mutations.

This fascinating intersection between molecular biology and evolutionary dynamics, published Jan. 22 on the cover of Molecular Cell, focuses on the most famous anti-cancer gene in the human body, TP53 (tumor protein 53, known as p53), and suggests that cancer cells don’t just mutate by accident — they create a specialized environment that makes dangerous mutations possible. 

The guardian under attack

Tasked with the job of stopping damaged cells from dividing, the p53 protein has been known for decades as the “guardian of the genome” and is the most mutated gene in cancer. Some of the most perilous of these mutations are known as “dominant-negative” variants. Not only do they stop working, but they actually prevent any healthy p53 in the cell from doing its job, essentially disarming the body’s primary defense system.

To function, p53 and most other proteins must fold into specific 3D shapes, much like precise cellular origami. Typically, if a mutation occurs that ruins this shape, the protein becomes a tangled mess, and the cell destroys it.

A specialized network of proteins, called cellular chaperones, help proteins fold into their correct shape, collectively known as the proteostasis network. 

“Many chaperone networks are known to be upregulated in cancer cells, for reasons that are not totally clear,” says Stephanie Halim, a graduate student in the Shoulders Group and co-first author of the study, along with Rebecca Sebastian PhD ’22. “We hypothesized that increasing the activities of these helpful protein folding networks can allow cancer cells to tolerate more mutations than a regular cell.”

The research team investigated a “helper” system in the cell called the proteostasis network. This network involves many proteins known as chaperones that help other proteins fold correctly. A master regulator called Heat Shock Factor 1 (HSF1) controls the composition of the proteostasis network, with HSF1 activity upregulating the network to create supportive protein folding environments in response to stress. In healthy cells, HSF1 stays dormant until heat or toxins appear. In cancer, HSF1 is often permanently in action mode.

To see how this works in real-time, the team created a specialized cancer cell line that let them chemically “turn up” the activity of HSF1 on demand. They then used a cutting-edge technique to express every possible singly mutated version of a p53 protein — testing thousands of different genetic “typos” at once.

The results were clear: When HSF1 was amplified, the cancer cells became much better at handling “bad” mutations. Normally, these specific mutations are so physically disruptive that they would cause the protein to collapse and fail. However, with HSF1 providing extra folding help, these unstable, cancer-driving proteins were able to stay intact and keep the cancer growing.

“These findings show that chaperone networks can reshape the fundamental mutational tolerance of the most mutated gene in cancer, linking proteostasis network activity directly to cancer development,” said Halim. “This work also puts us one step closer to understanding how tinkering with cellular protein folding pathways can help with cancer treatment.”

Unravelling cancer’s safety net

The study revealed that HSF1 activity specifically protects normally disruptive amino acid substitutions located deep inside the protein’s core — the most sensitive areas. Without this extra folding help, these substitutions would likely cause degradation of these proteins. With it, the cancer cell can keep these broken proteins around to help it grow.

This discovery helps explain why cancer is so resilient, and why previous attempts to treat cancer by blocking chaperone proteins (like HSP90, an abundant cellular chaperone) have been so complex. By understanding how cancer “buffers” its own bad mutations, doctors may one day be able to break that safety net, forcing the cancer’s own mutations to become its downfall.

The research was conducted in collaboration with the labs of professors Yu-Shan Lin of Tufts University; Francisco J. Sánchez-Rivera of the MIT Department of Biology; William C. Hahn, institute member of the Broad Institute of MIT and Harvard and professor of medicine in the Department of Medical Oncology at the Dana-Farber Cancer Institute and Harvard Medical School; and Marc L. Mendillo of Northwestern University.

MIT Professor Emeritus Richard O. Hynes PhD ’71, a cancer biologist whose discoveries reshaped modern understandings of how cells interact with each other and their environment, passed away on Jan. 6. He was 81.

Hynes is best known for his discovery of integrins, a family of cell-surface receptors essential to cell–cell and cell–matrix adhesion. He played a critical role in establishing the field of cell adhesion biology, and his continuing research revealed mechanisms central to embryonic development, tissue integrity, and diseases including cancer, fibrosis, thrombosis, and immune disorders.

Hynes was the Daniel K. Ludwig Professor for Cancer Research, Emeritus, an emeritus professor of biology, and a member of the Koch Institute for Integrated Cancer Research at MIT and the Broad Institute of MIT and Harvard. During his more than 50 years on the faculty at MIT, he was deeply respected for his academic leadership at the Institute and internationally, as well as his intellectual rigor and contributions as an educator and mentor.

“Richard had an enormous impact in his career. He was a visionary leader of the MIT Cancer Center, what is now the Koch Institute, during a time when the progress in understanding cancer was just starting to be translated into new therapies,” reflects Matthew Vander Heiden, director of the Koch Institute and the Lester Wolfe (1919) Professor of Molecular Biology. “The research from his laboratory launched an entirely new field by defining the molecules that mediate interactions between cells and between cells and their environment. This laid the groundwork for better understanding the immune system and metastasis.”

Pond skipper

Born in Kenya, Hynes grew up during the 1950s in Liverpool, in the United Kingdom. While he sometimes recounted stories of being schoolmates with two of the Beatles, and in the same Boy Scouts troop as Paul McCartney, his academic interests were quite different, and he specialized in the sciences at a young age. Both of his parents were scientists: His father was a freshwater ecologist, and his mother a physics teacher. Hynes and all three of his siblings followed their parents into scientific fields.

"We talked science at home, and if we asked questions, we got questions back, not answers. So that conditioned me into being a scientist, for sure," Hynes said of his youth.

He described his time as an undergraduate and master’s student at Cambridge University during the 1960s as “just fantastic,” noting that it was shortly after two 1962 Nobel Prizes were awarded to Cambridge researchers — one to Francis Crick and James Watson for the structure of DNA, the other to John Kendrew and Max Perutz for the structures of proteins — and Cambridge was “the place to be” to study biology.

Newly married, Hynes and his wife traded Cambridge, U.K. for Cambridge, Massachusetts, so that he could conduct doctoral work at MIT under the direction of Paul Gross. He tried (and by his own assessment, failed) to differentiate maternal messages among the three germ layers of sea urchin embryos. However, he did make early successful attempts to isolate the globular protein tubulin, a building block for essential cellular structures, from sea urchins.

Inspired by a course he had taken with Watson in the United States, Hynes began work during his postdoc at the Institute of Cancer Research in the U.K. on the early steps of oncogenic transformation and the role of cell migration and adhesion; it was here that he made his earliest discovery and characterizations of the fibronectin protein.

Recruited back to MIT by Salvador Luria, founding director of the MIT Center for Cancer Research, whom he had met during a summer at Woods Hole Oceanographic Institute on Cape Cod, Hynes returned to the Institute in 1975 as a founding faculty member of the center and an assistant professor in the Department of Biology.

Big questions about tiny cells

To his own research, Hynes brought the same spirit of inquiry that had characterized his upbringing, asking fundamental questions: How do cells interact with each other? How do they stick together to form tissues?

His research focused on proteins that allow cells to adhere to each other and to the extracellular matrix — a mesh-like network that surrounds cells, providing structural support, as well as biochemical and mechanical cues from the local microenvironment. These proteins include integrins, a type of cell surface receptor, and fibronectins, a family of extracellular adhesive proteins. Integrins are the major adhesion receptors connecting the extracellular matrix to the intracellular cytoskeleton, or main architectural support within the cell.

Hynes began his career as a developmental biologist, studying how cells move to the correct locations during embryonic development. During this stage of development, proper modulation of cell adhesion is critical for cells to move to the correct locations in the embryo.

Hynes’ work also revealed that dysregulation of cell-to-matrix contact plays an important role in cancer cells’ ability to detach from a tumor and spread to other parts of the body, key steps in metastasis.

As a postdoc, Hynes had begun studying the differences in the surface landscapes of healthy cells and tumor cells. It was this work that led to the discovery of fibronectin, which is often lost when cells become cancerous.

He and others found that fibronectin is an important part of the extracellular matrix. When fibronectin is lost, cancer cells can more easily free themselves from their original location and metastasize to other sites in the body. By studying how fibronectin normally interacts with cells, Hynes and others discovered a family of cell surface receptors known as integrins, which function as important physical links with the extracellular matrix. In humans, 24 integrin proteins have been identified. These proteins help give tissues their structure, enable blood to clot, and are essential for embryonic development.

“Richard’s discoveries, along with others’, of cell surface integrins led to the development of a number of life-altering treatments. Among these are treatment of autoimmune diseases such as multiple sclerosis,” notes longtime colleague Phillip Sharp, MIT Institute professor emeritus.

As research technologies advanced, including proteomic and extracellular matrix isolation methods developed directly in Hynes’ laboratory, he and his group were able to uncover increasingly detailed information about specific cell adhesion proteins, the biological mechanisms by which they operate, and the roles they play in normal biology and disease.

In cancer, their work helped to uncover how cell adhesion (and the loss thereof) and the extracellular matrix contribute not only to fundamental early steps in the metastatic process, but also tumor progression, therapeutic response, and patient prognosis. This included studies that mapped matrix protein signatures associated with cancer and non-cancer cells and tissues, followed by investigations into how differentially expressed matrix proteins can promote or suppress cancer progression. 

Hynes and his colleagues also demonstrated how extracellular matrix composition can influence immunotherapy, such as the importance of a family of cell adhesion proteins called selectins for recruiting natural killer cells to tumors. Further, Hynes revealed links between fibronectin, integrins, and other matrix proteins with tumor angiogenesis, or blood vessel development, and also showed how interaction with platelets can stimulate tumor cells to remodel the extracellular matrix to support invasion and metastasis. In pursuing these insights into the oncogenic mechanisms of matrix proteins, Hynes and members of his laboratory have identified useful diagnostic and prognostic biomarkers, as well as therapeutic targets.

Along the way, Hynes shaped not only the research field, but also the careers of generations of trainees.

“There was much to emulate in Richard’s gentle, patient, and generous approach to mentorship. He centered the goals and interests of his trainees, fostered an inclusive and intellectually rigorous environment, and cared deeply about the well-being of his lab members. Richard was a role model for integrity in both personal and professional interactions and set high expectations for intellectual excellence,” recalls Noor Jailkhani, a former Hynes Lab postdoc.

Jailkhani is CEO and co-founder, with Hynes, of Matrisome Bio, a biotech company developing first-in-class targeted therapies for cancer and fibrosis by leveraging the extracellular matrix. “The impact of his long and distinguished scientific career was magnified through the generations of trainees he mentored, whose influence spans academia and the biotechnology industry worldwide. I believe that his dedication to mentorship stands among his most far-reaching and enduring contributions,” she says.

A guiding light

Widely sought for his guidance, Hynes served in a number of key roles at MIT and in the broader scientific community. As head of MIT’s Department of Biology from 1989 to 1991, then a decade as director of the MIT Center for Cancer Research, his leadership has helped shape the Institute’s programs in both areas.

“Words can’t capture what a fabulous human being Richard was. I left every interaction with him with new insights and the warm glow that comes from a good conversation,” says Amy Keating, the Jay A. Stein (1968) Professor, professor of biology and biological engineering, and head of the Department of Biology. “Richard was happy to share stories, perspectives, and advice, always with a twinkle in his eye that conveyed his infinite interest in and delight with science, scientists, and life itself. The calm support that he offered me, during my years as department head, meant a lot and helped me do my job with confidence.”

Hynes served as director of the MIT Center for Cancer Research from 1991 until 2001, positioning the center’s distinguished cancer biology program for expansion into its current, interdisciplinary research model as MIT’s Koch Institute for Integrative Cancer Research. “He recruited and strongly supported Tyler Jacks to the faculty, who subsequently became director and headed efforts to establish the Koch Institute,” recalls Sharp.

Jacks, a David H. Koch (1962) Professor of Biology and founding director of the Koch Institute, remembers Hynes as a thoughtful, caring, and highly effective leader in the Center for Cancer Research, or CCR, and in the Department of Biology. “I was fortunate to be able to lean on him when I took over as CCR director. He encouraged me to drop in — unannounced — with questions and concerns, which I did regularly. I learned a great deal from Richard, at every level,” he says.

Hynes’ leadership and recognition extended well beyond MIT to national and international contexts, helping to shape policy and strengthen connections between MIT researchers and the wider field. He served as a scientific governor of the Wellcome Trust, a global health research and advocacy foundation based in the United Kingdom, and co-chaired U.S. National Academy committees establishing guidelines for stem cell and genome editing research.

“Richard was an esteemed scientist, a stimulating colleague, a beloved mentor, a role model, and to me a partner in many endeavors both within and beyond MIT,” notes H. Robert Horvitz, a David H. Koch (1962) Professor of Biology. He was a wonderful human being, and a good friend. I am sad beyond words at his passing.”

Awarded Howard Hughes medical investigator status in 1988, Hynes’ research and leadership have since been recognized with a number of other notable honors. Most recently, he received the 2022 Albert Lasker Basic Medical Research Award, which he shared with Erkki Ruoslahti of Sanford Burnham Prebys and Timothy Springer of Harvard University, for his discovery of integrins and pioneering work in cell adhesion.

His other awards include the Canada Gairdner International Award, the Distinguished Investigator Award from the International Society for Matrix Biology, the Robert and Claire Pasarow Medical Research Award, the E.B. Wilson Medal from the American Society for Cell Biology, the David Rall Medal from the National Academy of Medicine and the Paget-Ewing Award from the Metastasis Research Society. Hynes was a member of the National Academy of Sciences, the National Academy of Medicine, the Royal Society of London, the American Association for the Advancement of Science, and the American Academy of Arts and Sciences.

Easily recognized by a commanding stature that belied his soft-spoken nature, Hynes was known around MIT’s campus not only for his acuity, integrity, and wise counsel, but also for his community spirit and service. From serving food at community socials to moderating events and meetings or recognizing the success of colleagues and trainees, his willingness to help spanned roles of every size.

“Richard was a phenomenal friend and colleague. He approached complex problems with a thoughtfulness and clarity that few can achieve,” notes Vander Heiden. “He was also so generous in his willingness to provide help and advice, and did so with a genuine kindness that was appreciated by everyone.”

Hynes is survived by his wife Fleur, their sons Hugh and Colin and their partners, and four grandchildren.

Really interesting blog post from Anthropic:

In a recent evaluation of AI models’ cyber capabilities, current Claude models can now succeed at multistage attacks on networks with dozens of hosts using only standard, open-source tools, instead of the custom tools needed by previous generations. This illustrates how barriers to the use of AI in relatively autonomous cyber workflows are rapidly coming down, and highlights the importance of security fundamentals like promptly patching known vulnerabilities.

[…]

A notable development during the testing of Claude Sonnet 4.5 is that the model can now succeed on a minority of the networks without the custom cyber toolkit needed by previous generations. In particular, Sonnet 4.5 can now exfiltrate all of the (simulated) personal information in a high-fidelity simulation of the Equifax data breach—­one of the costliest cyber attacks in history—­using only a Bash shell on a widely-available Kali Linux host (standard, open-source tools for penetration testing; not a custom toolkit). Sonnet 4.5 accomplishes this by instantly recognizing a publicized CVE and writing code to exploit it without needing to look it up or iterate on it. Recalling that the original Equifax breach happened by exploiting a publicized CVE that had not yet been patched, the prospect of highly competent and fast AI agents leveraging this approach underscores the pressing need for security best practices like prompt updates and patches. ...