ReviewNature reviews. Molecular cell biology2026
The mechanistic basis and cellular functions of UFMylation.
Review in Nature reviews. Molecular cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Ubiquitin and ubiquitin-like modifications in the endoplasmic reticulum stress response.The FEBS journal · 2026Review
- A Practical Experimental Protocol for Identification and Validation of UFMylation Substrate in Human Cells.Bio-protocol · 2026Article
- Evaluating evidence for UFMylation client diversity.Nature reviews. Molecular cell biology · 2026Article
- A severe neurodevelopmental syndrome linked to a South Asian founder variant in the UFMylation adaptor CDK5RAP3.Acta neuropathologica · 2026Article
- UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism.bioRxiv : the preprint server for biology · 2026Article
- SQSTM1/p62 UFMylation Enhances Autophagic Clearance of Pathogenic Mutant Huntingtin.International journal of biological sciences · 2026Article
- UFM1 at the endoplasmic reticulum: linking ER stress, ribosome quality control, and ER-phagy.Essays in biochemistry · 2025Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UFMylation is a ubiquitin-like post-translational modification that has a central role in ribosome-associated quality control at the endoplasmic reticulum (ER-RQC). Through a dedicated enzymatic cascade, UFM1 is conjugated to select substrates, notably the 60S ribosomal subunit protein RPL26, to maintain endoplasmic reticulum and ribosomal integrity under cellular stress. This Review focuses on the structural and mechanistic basis of UFMylation in ER-RQC and its contribution to proteostasis. Although recent studies have identified a growing number of putative UFM1-modified proteins across diverse cellular pathways, the physiological importance of many of these substrates remains unclear. We highlight both the emerging functional breadth of UFMylation and the need for caution in interpreting substrate relevance. UFMylation is increasingly linked to disease, including neurodevelopmental disorders and cancer, underscoring its biological importance. Together, these findings position UFMylation as a key regulatory system connecting endoplasmic reticulum function to broader stress responses.
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Registered trials
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