ReviewEssays in biochemistry2025
UFM1 at the endoplasmic reticulum: linking ER stress, ribosome quality control, and ER-phagy.
Review in Essays in biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Ubiquitin and ubiquitin-like modifications in the endoplasmic reticulum stress response.The FEBS journal · 2026Review
- A 3D RNA-protein proximity ligation protocol detecting the heterogeneity of LISRR-RPL26 interactions in patient-derived melanoma tumor explants.STAR protocols · 2026Article
- The UFM1 Conjugation System: A Master Regulator of Cellular Stress Surveillance in Human Disease.Biology · 2026Review
- From molecular logic to therapeutic modulation: advances in Ub/UBL signalling.Essays in biochemistry · 2025Article
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Authors and funding
2 authors.
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Abstract
Ubiquitin-fold modifier 1 (UFM1) is a small protein that functions as a ubiquitin-like modifier attached to other proteins to alter their behavior. Although less famous than ubiquitin, UFM1 has gained attention as a key regulator of proteostasis (protein homeostasis) in the cell. Notably, the endoplasmic reticulum (ER) has emerged as the central stage for UFM1's activity. UFM1 was initially recognized for its role in the ER stress response, and we now know it orchestrates two critical quality-control processes at the ER: ribosome-associated quality control and selective autophagy of the ER. Together, these mechanisms ensure that the cell can cope with misfolded proteins and stalled ribosomes, maintaining the health of the ER and the proteins it produces. In this review, we will explore how UFM1 works at the ER, how its components are regulated during stress, how it facilitates both immediate quality control and longer-term ER turnover, and how disruptions in this system lead to disease, especially in the nervous system.
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