ArticleScientific reports2017
Novel insights into the interaction of UBA5 with UFM1 via a UFM1-interacting sequence.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Discovery and Characterization of Inhibitors of Ubiquitin-Like Modifier Activating Enzyme 5 (UBA5): Targeting the UFMylation Pathway in Cancer and Neurodegenerative Diseases.ACS chemical biology · 2026Article
- The UFM1 Conjugation System: A Master Regulator of Cellular Stress Surveillance in Human Disease.Biology · 2026Review
- UFMylation System: Biological Functions, Molecular Mechanisms, Diseases, and Drug Discovery.MedComm · 2025Review
- The rapidly expanding role of LC3-interacting regions in autophagy.The Journal of cell biology · 2025Review
- Article
- Article
- Allelic strengths of encephalopathy-associatedeLife · 2023Article
- Review
- Mechanistic insights into the roles of the UFM1 E3 ligase complex in ufmylation and ribosome-associated protein quality control.Science advances · 2023Article
- Shuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and autophagy.The EMBO journal · 2023Article
- A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation.The EMBO journal · 2022Article
- Article
- Overexpression of UBA5 in Cells Mimics the Phenotype of Cells Lacking UBA5.International journal of molecular sciences · 2022Article
- Structural basis for UFM1 transfer from UBA5 to UFC1.Nature communications · 2021Article
- A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1.International journal of molecular sciences · 2021Article
- Highly Specialized Ubiquitin-Like Modifications: Shedding Light into the UFM1 Enigma.Biomolecules · 2021Review
- Decrypting UFMylation: How Proteins Are Modified with UFM1.Biomolecules · 2020Review
- The UFMylation System in Proteostasis and Beyond.Trends in cell biology · 2019Review
- UFM1-Activating Enzyme 5 (Uba5) Requires an Extension to Get the Job Done Right.Journal of molecular biology · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The modification of proteins by ubiquitin-fold modifier 1 (UFM1) is implicated in many human diseases. Prior to conjugation, UFM1 undergoes activation by its cognate activating enzyme, UBA5. UBA5 is a non-canonical E1 activating enzyme that possesses an adenylation domain but lacks a distinct cysteine domain. Binding of UBA5 to UFM1 is mediated via an amino acid sequence, known as the UFM1-interacting sequence (UIS), located outside the adenylation domain that is required for UFM1 activation. However, the precise boundaries of the UIS are yet not clear and are still under debate. Here we revisit the interaction of UFM1 with UBA5 by determining the crystal structure of UFM1 fused to 13 amino acids of human UBA5. Using binding and activity assays, we found that His 336 of UBA5, previously not reported to be part of the UIS, occupies a negatively charged pocket on UFM1's surface. This His is involved in UFM1 binding and if mutated perturbs activation of UFM1. Surprisingly, we also found that the interaction between two UFM1 molecules mimics how the UIS binds UFM1. Specifically, UFM1 His 70 resembles UBA5 His336 and enters a negatively charged pocked on the other UFM1 molecule. Our results refine our understanding of UFM1-UBA5 binding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.