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Influenza virus, shown here coloured red inside lung cells, infects these and other epithelial cells of the respiratory tract to create all the unpleasant symptoms we associate with a bout of flu. Recently, scientists who were investigating how the virus is replicated and mobilised within these cells made a surprising discovery. They inhibited the activity of a particular vesicle [a membrane-coated organelle for moving molecules in and out of cells] trafficking protein, called Rab11B, to see the effect on viral protein transport and found that one of the viral strains they were studying (H3N2) was blocked from entering the cells altogether. The other (H1N1) was not. Until these experiments, it had been presumed that H3N2 and H1N1 entered cells by the same mechanism. While the precise role of Rab11B in H3N2 cellular entry remains to be determined, the findings could lead to new ways for preventing and curtailing infections with that particular strain.

Written by Ruth Williams

Image from work by Allyson H. Turner & Sara A. Jaffrani, and colleagues, Bruce Lab

Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont, USA

Image originally published with no restrictions – hence published here with as Creative Commons Attribution 4.0 International (CC BY 4.0)

Research published in Journal of Virology, June 2026

Loophole for Entry

A common route for cancer cell spread or metastasis is via lymphatics – the vessels that connect the body-wide network of lymph tissue, sites of immune response. This report finds entry by the cancer cells into the lympho-vascular system is driven by the balance of TNRC6B/circTNRC6B gene products (an interactive self-degradative loop of TNRC6B protein and a circular product of the TNRC6B gene message); their activity could be a biomarker of prognosis and a treatment target

Read the published research article here

Image from work by Lingjiao Meng, Haotian Wu & Jiaxiang Wu, and colleagues

Fourth Hospital of Hebei Medical University, Shijiazhuang, Hebei, China

Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)

Published in Cell Reports, July 2026

Controlled by Axin

Immediately after implantation, formation of the embryo begins. From early cells called the pluripotent epiblast, the differentiation into the myriad cell types of the body begins to unfold, first into a layer called the mesoderm, but how this specification is controlled remains to be fully elucidated. The Wnt signalling pathway of molecules underlies the steps towards specific cell type commitment, and here, a study of mouse embryo development reveals that proteins AXIN1 and AXIN2 regulate Wnt to prevent the epiblast committing to mesoderm differentiation until the time is right

Read the published research article here

Image from work by Rocío Hernández-Martínez and colleagues

Developmental Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, USA

Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)

Published in Developmental Cell, July 2026

Seams Vital

Like the carefully stitched hem of a pleated skirt, the outer layer of the heart is fundamental to its entire shape and function. This epicardium is a regulator of development and regeneration, and supports vessel and muscle growth. To better understand the molecular mechanisms guiding its development, researchers investigated a protein called SRSF3, which helps process RNA messages (strands of genetic material). When it was removed from early mouse epicardial precursor cells, the epicardium failed to form normally (right, reduced green SRSF3 limiting outgrowth around explants cultured from embryonic hearts, compared to normal, left) so proper heart formation was prevented. Their experiments also showed cells that dodged SRSF3 deletion increased production to compensate, cautioning researchers that incomplete gene deletion can hide how important a gene really is in experiments. Understanding these growth controls could eventually help researchers tackle both congenital heart defects and the challenge of repairing broken hearts.

Written by Anthony Lewis

Image from work by Irina-Elena Lupu and Susann Bruche, and colleagues

Institute of Developmental and Regenerative Medicine, British Heart Foundation Centre of Research Excellence, Department of Physiology, Anatomy and Genetics, University of Oxford, Oxford, UK

Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)

Published in Development, March 2026

Variety Upon Variety

Titin, the largest protein produced in the body, is a giant spring-like protein found in muscle cells, including those of the heart (pictured). There are multiple versions of titin, and their production is regulated, at least in part, by splicing factor (cutting the RNA transcript to make different sized versions of the same protein) RBM20 (coloured blue). In the infant mammalian heart, for example, most titin is long and elastic, while in older mammals RBM20 activity leads to shorter stiffer versions of the protein. Aberrant production of RBM20 has been linked to certain cardiomyopathies, suggesting its inhibition in these disorders could be clinically beneficial. Interestingly, new research in rodent and human samples reveals RBM20 itself also has multiple versions, and their production is influenced by developmental stage and disease. The findings suggest regulation of heart muscle flexibility is much more complex than previously thought and that any therapies targeting RBM20 might need fine tuning to pinpoint specific versions of the factor.

Written by Ruth Williams

Image from work by Michael H. Radke, Victor Badillo Lisakowski and Stefan Meinke, and colleagues

Translational Cardiology and Functional Genomics, Max Delbrück Center for Molecular Medicine, Berlin, Germany

Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)

Published in Nature Communications, May 2026

Metal Liker Unforgiven

We need trace metals for healthy cell function but then so do all other organisms, handily we have a means of safeguarding the supply of certain metals which doubles as an anti-pathogen strategy. A protein in the mammalian gut lining cells called natural resistance-associated macrophage protein 2 (also known as SLC11A2) starves pathogenic microrganisms of iron and manganese – shown here using Salmonella enterica (in red) as a model in cow gut, with metals tracked using fluorescent sensors

Read the published research article here

Image from work by Emilia S. Norberg and colleagues

Department of Microbiology and Molecular Genetics, Robert Larner, M.D. College of Medicine, University of Vermont, Burlington, VT, USA

Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)

Published in Proceedings of the National Academy of Science (PNAS), June 2026

Arbor Mastered

Assembling and growing in the lab the different cell types that make up a particular body tissue – cultures known as organoids – emulates physiology in many ways sufficiently to study cell and molecular interactions for example, but there's more to life. Here, using a defined chemical protocol, lung organoids have been coaxed to branch, mimicking the tree-like pattern seen in our lungs, upgrading to a more life-like means to study development and regeneration

Read the published research article here

Image from work by Mengjie Pan, Baomei Cai, Guanlie Li, Ruifang Zhang, Chuncao Deng, Huan Chen and colleagues

Guangzhou National Laboratory, The Fifth Affiliated Hospital of Guangzhou Medical University, Guangzhou, Guangdong, China

Image originally published with a Creative Commons Attribution – NonCommercial – NoDerivs (CC BY-NC-ND 4.0)

Published in Developmental Cell, June 2026

Unexpected Barrier Function

All eukaryotic organisms – that is, all animals, plants and fungi – contain a protein called cyclin dependent kinase 1 (CDK1), which is critical for driving cells through the process of division. This role in cell division has been known for about fifty years, but recent research reveals that CDK1 has another hitherto unknown function. Scientists studying mammalian kidney epithelial cells (pictured) discovered that the protein was located at intercellular connections (green) where it interacted with cell-to-cell cohesion factors and promoted epithelial barrier integrity. Indeed, inhibiting CDK1 activity led to perturbed cell contacts and caused areas of the barrier to become leaky (purple regions). Because of CDK1’s role in the cell cycle, the protein has been proposed as a potential target for cancer therapy. Investigations into such therapies, should thus keep in mind CDK1’s newly discovered function and the implications of its disruption.

Written by Ruth Williams

Image by from Margarida Dantas and Martijn Gloerich. Re: work by Margarida Dantas & Lisa Donker, and colleagues

Center for Molecular Medicine, University Medical Center Utrecht, Utrecht, Netherlands

Image copyright held by the original authors

Research published in Science Signaling, June 2026