Hundreds of scientists who study cancer and aging have made an easily avoidable but significant mistake, deploying the wrong antibody to test for a key protein, according to a researcher who exposes errors in the biomedical literature. Learn more: scim.ag/4akPaP4 @NewsfromScience

J for Junction: Adherens junctions are cell-cell adhesion complexes where transmembrane cadherins bind to neighboring cells and connect intracellularly to the actin cytoskeleton. This linkage is mediated by a protein network including catenins, vinculin, and α-actinin.

🚨 BREAKING: A "holy grail" moment for lung cancer prevention. Funded in part by a @TheMarkFdn ASPIRE Award & published in @CellCellPress, @CharlesSwanton & team have discovered a 14-protein blood signature that can predict lung cancer risk over 5 years before a diagnosis. 🧵👇 themarkfoundation.org/portfo…

Today I'm posting a new blog about an astonishing scientific own goal. Hundreds of papers have reported using a completely wrong antibody to investigate the tumor suppressor p16. This mistake has happened because scientists have muddled the names of two proteins 🧵

Another sign of Illinois’ growing importance as a leading life science hub. We’re fostering research, science, and attracting more good-paying jobs. chicagobusiness.com/health-c…

"Human hepatocytes show continuous and lifelong turnover, allowing the liver to remain a young organ (average age <3 years)." Yet, "physiological liver cell renewal in humans is mainly dependent on diploid hepatocytes, whereas polyploid cells are compromised in their ability to divide." We get more polyploid cells as we age, and limit the ability of the liver to regenerate (at least so far): cell.com/cell-systems/fullte….

The winner of our 2025 JCS-David Stephens Prize is Jason Casler @JasonCasler1 for his paper entitled ‘Mitochondria plasma membrane contact sites regulate the ER mitochondria encounter structure’ with Laura Lackner. journals.biologists.com/jcs/…

Publishing in JCB enables authors funded by National Institutes of Health (NIH), Howard Hughes Medical Institute (HHMI), and other funders an easy pathway to compliance. Learn more: hubs.la/Q048mlnf0

Visibility in Academia, like in the world, is not fixed; it is produced. This piece “What Cell Biology Reveals About Academia” is a reminder that everyone has the potential to be either seen or unseen.    sciencepolitics.org/2026/03/…

We’re proud to share that Luisa Morales‑Nebreda, MD, has been named a 2026 Young Physician‑Scientist Awardee by the American Society for Clinical Investigation. This national honor recognizes her outstanding research achievements and commitment to advancing biomedical science. 🔗 See more: breakthroughsforphysicians.n…

🌈 Download JCB's CELLULAR DIVERSITY poster! 📩 Sign up to receive our future special collections and download this beautiful artwork by Bianca Dunn to display at home or in the lab 👉 hubs.la/Q03_C0Jq0

I will be presenting at Consortium for Top-Down Proteomics’s Proteoform Thursday Webinar Series. The catenin phospho-code work laid the foundation for my future research group. Free register link below!

Are you headed to @GordonConf #GRC #Autophagy in Stress, Development and Disease next week, and interested in speaking with a JCB Editor about publishing your work? Get in touch with our Executive Editor, Tim Spencer, who will be there! ✉️ Email Tim: hubs.la/Q046glnp0

#FusionLung26 ECR Networking Lunch. Great to see students and postdocs connecting with leaders in the field over our ECR networking lunch today. So many great conversations surrounding research and career paths with some of our industry and academic speakers! Exactly what networking should look like 🍹🥗🔬

So much of life is mechanical: T-cell activation, antibody maturation, pathogenesis, development, homeostasis, and more. They all rely on molecular force sensing. Expanding throughput is the first step for unlocking the potential of engineered molecular force responses. 11/13

📣 Paper alert! The Landino Lab's first peer-reveiwed research article is officially online! We are happy this work found a home in MBoC. Congratulations to Greg, and thank you to the many people who helped get us here! Check it out here: molbiolcell.org/doi/abs/10.1…

We need more investment in broad-spectrum antivirals, or medicines that defend people against many viruses simultaneously. Unfortunately, it’s hard to do this! There are more than 60 types of adenovirus alone, for example, each carrying unique proteins. Designing an antiviral that blocks all of these is very difficult. Instead of designing drugs, then, what if we harnessed physics? After all, every virus enters a human cell by “pressing” or “pushing” on it. If the cell can sense these physical forces, and somehow use them to trigger resistance, then perhaps we could develop more universal antivirals. A new paper hints at this possibility, and it stems from a weird discovery that came before. A few years ago, scientists grew human cells at low densities and infected them with viruses. When they did this, each cell produced large amounts of the virus; they were easily infected. When this experiment was repeated with cells grown at a high density, though, each cell (on average) produced much less virus. Something with this “crowding” was blocking viral replication. These scientists speculated that a protein, called Piezo1, might be involved. Piezo1 is a mechanically-sensitive calcium channel. Upon activation (with vibrations, touch, or small molecules) it opens, allowing calcium to pour into the cell. This calcium influx then causes the cell membrane to stiffen, though the mechanism for this is not clear. For this new paper, then, Chinese scientists grew human cells at low or high densities, infected them with many different viruses, and studied Piezo1’s involvement. When they grew cells at high density, but knocked out Piezo1, each cell produced more viruses. Similarly, when cells were grown at a low density and infected with viruses, while being shaken on a plate, they became more resistant to infection. This effect disappeared when Piezo1 was deleted. Similarly, when the authors overexpressed Piezo1 in HEK293T cells, it suppressed viral replication (by about 10-fold). This effect was not observed with Piezo2, another mechanosensitive ion channel. The researchers next used Piezo1 agonists to simulate this effect. A small molecule, called Yoda1, binds and activates Piezo1. Treating cells with Yoda1 reduced viral titers in human cells by 10-100 fold. The researchers also infected mice with lethal doses of various viruses (enteroviruses, coxsackievirus, influenza A), treated the animals with Yoda1 (or controls), and found that treated mice were more likely to survive. This work is interesting, but also flawed. For one, the molecular mechanism linking Piezo1 —> viral resistance is not described. They think it has something to do with membrane stiffening, but nobody actually knows *how* Piezo1 activation causes this. Another issue is the methods. For one experiment, the researchers infected mice with viruses and then shook them on little platforms. This, apparently, increased their resistance. But the scientists never actually explain the method, or what the platforms look like, or what the device settings were. It’s all a bit vague and difficult to believe. Still, searching for “universal” or physical mechanisms to build broad-spectrum therapies is exciting. Rather than make small molecules that target one pathogen, we ought to think about unifying, biophysical principles that can be used to exert control more widely.

There is a special kind of joy in research that doesn’t come from publishing a research article or scaling a dataset to millions of points. It comes from understanding. From the moment when a pattern is no longer just a correlation, but a mechanism. When a result is not just statistically significant, but conceptually illuminating. When what you learned in one system suddenly generalizes to many. We live in an era of ever larger datasets and increasingly powerful models. Scale is intoxicating. But scale alone is not insight. More data does not automatically mean deeper understanding. The joy of science is not just in predicting outcomes. It is in discovering why they arise, and when they must hold across systems. It is in building explanations that are robust, falsifiable, and transferable. If we short-circuit that process -- if we optimize only for size, speed, and output -- we risk losing something essential. The next generation deserves more than technical proficiency. They deserve to experience the exhilaration of figuring something out, of seeing nature yield a principle that was always there, waiting to be understood. And this joy is not reserved for scientists. It is one of the most meaningful ways humans engage with the world. Understanding is not a luxury. It is one of the deepest forms of appreciation.

β-catenin condensation facilitates clustering of the cadherin/catenin complex and formation of nascent cell-cell junctions nature.com/articles/s41467-0…

Membrane rupture and independent extension of sister membranes drive cytokinesis in C. elegans embryos biorxiv.org/content/10.1101/…