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Originally published by Katherine Fenz, Rockefeller University, on Jun 5, 2025 edited by Lisa Lock , reviewed by Andrew Zinin Three dimensional cryo-EM structure of VCP (blue and purple) bound to three VCPIP1 promoters (red, orange, and yellow). Credit: Kapoor lab Healthy cells are constantly breaking down proteins and building up new ones with the help of enzymes aptly named unfoldases , because they unravel proteins tagged for destruction or recycling . Now, a new electron microscopy study demonstrates how VCP, one such unfoldase , physically interacts with tag removal enzymes, called DUBs . The findings show how these two enzymes work in tandem to process proteins , and may have implications for the study of diseases such as those linked to neurodegeneration . The research is published in the Journal of Cell Biology . "VCP dysfunction is linked to neurodegenerative disorders, such as Alzheimer's," says first author Lauren Vostal, a graduate student in the ...

Autism and ADHD have distinct brain connectivity signatures, study finds Originally published by Ingrid Fadelli , at Phys.org, on May 31, 2025   edited by Stephanie Baum , reviewed by Robert Egan Comparative analysis of brain connectivity in autism and ADHD. Credit: Nature Mental Health (2025). DOI: 10.1038/s44220-025-00431-5 Autism spectrum disorder ( ASD ) a nd attention-deficit/hyperactivity disorder ( ADHD ) are among the most well-known neurodevelopmental conditions , estimated to affect approximately 1–3% and 5–7% of the global population , respectively. While people diagnosed with ASD can experience difficulties with social communication, repetitive behaviors and a heightened sensitivity to sensory stimuli (e.g., lights, sounds, etc.), those diagnosed with ADHD are often prone to hyperactivity, impulsivity and inattention , which makes it harder for them to focus on tasks for extended periods of time. ADHD and autism often co-occur , with statistics estimati...

Originally published by Universitätsmedizin Göttingen, on May 28, 2025 edited by Gaby Clark , reviewed by Robert Egan Cryo-EM micrograph (left) of myoferlin particles (with one particle highlighted circle). 3D reconstruction of the myoferlin structure (right), with compact ring-like arrangement of the various key domains (colored) achieved upon membrane binding. Credit: Biological Reviews (2025). DOI: 10.1111/brv.70032 Researchers from the Göttingen Cluster of Excellence Multiscale Bioimaging (MBExC) have uncovered the 3D structure of the membrane proteins myoferlin and dysferlin using high-resolution cryo-electron microscopy. The findings enable new approaches for the development of targeted drugs for the treatment of diseases such as muscle atrophy, hearing disorders and certain cancers . The results have been published in The EMBO Journal . Read more