Study Links UFMylation to Protein Damage Defense
Israeli and Chinese researchers found that reducing a cellular process strengthened worms' natural defenses against harmful proteins.
Updated on Nov. 3, 2026 in Life Sciences
Researchers from the Hebrew University of Jerusalem and the National Institute of Biological Sciences in Beijing identified UFMylation, a cellular process that influences how cells protect themselves against damaged proteins. The findings, published in Nature Communications, were drawn from experiments on the microscopic worm Caenorhabditis elegans.
Why it matters
As cells age, they become less effective at dealing with damaged and misfolded proteins, a process linked to conditions such as Alzheimer's disease. The study suggests that any potential treatment would need to adjust UFMylation carefully rather than block it altogether.
In a microscopic worm model, reducing UFMylation lowered paralysis by approximately 35 percent in an Alzheimer's disease model and extended lifespan by about 13 percent among worms carrying toxic proteins. The researchers identified 155 proteins affected by the process, but the worms do not develop the human conditions themselves.
The players
Prof. Ehud Cohen
Prof. Ehud Cohen leads the Institute for Medical Research Israel-Canada at the Hebrew University of Jerusalem's Faculty of Medicine, where he led the study.
Hebrew University of Jerusalem
The Hebrew University of Jerusalem is one of Israel's leading research universities, with a medical faculty that conducted the study.
National Institute of Biological Sciences
The National Institute of Biological Sciences is a research institute in Beijing, China, that collaborated on the study.
The details
Reducing UFMylation activity strengthened several natural defenses against damaged and misfolded proteins, improving quality control of newly produced proteins, reducing harmful protein clumps and increasing the breakdown and removal of damaged proteins. Completely eliminating UFMylation, however, impaired human cells' ability to manage damaged proteins.
Timeline
Findings were reported in Nature Communications; the date of publication is not specified in the source material.
Big Picture
Caenorhabditis elegans has long served as a model organism for studying aging and protein misfolding, and this study uses it to examine UFMylation, a pathway that had received less attention in that line of research. The findings add a specific cellular mechanism to the broader effort to understand how cells lose protein quality control with age.
The findings point toward future research into adjusting UFMylation carefully as a possible approach to protein-damage diseases, though any treatment is far from clinical use. For now, the results inform laboratory science rather than changing care for patients.
The takeaway
Cellular quality control declines with age, and the study shows that tuning a specific pathway, rather than eliminating it, may be key to strengthening defenses against damaged proteins.
Further reading
Explore more research on cellular biology in our Life Sciences section.
