ArticleNature communications2016
A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Statins attenuate PD-L1 sorting to small extracellular vesicles dependent on ubiquitin-like 3 modification.Scientific reports · 2025Article
- Intracellular dynamics of ubiquitin-like 3 visualized using an inducible fluorescent timer expression system.Biology open · 2024Article
- Ubiquitin-like protein 3 (UBL3) is required for MARCH ubiquitination of major histocompatibility complex class II and CD86.Nature communications · 2022Article
- Ubiquitin-like 3 as a new protein-sorting factor for small extracellular vesicles.Cell structure and function · 2022Review
- The Structure of theFrontiers in cell and developmental biology · 2022Article
- Structural and Functional Analysis of Ubiquitin-based Inhibitors That Target the Backsides of E2 Enzymes.Journal of molecular biology · 2020Article
- Post-translational modification and protein sorting to small extracellular vesicles including exosomes by ubiquitin and UBLs.Cellular and molecular life sciences : CMLS · 2019Review
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- DENEDDYLASE1 Protein Counters Automodification of Neddylating Enzymes to Maintain NEDD8 Protein Homeostasis inThe Journal of biological chemistry · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Ubiquitin (Ub) is a protein modifier that controls processes ranging from protein degradation to endocytosis, but early-acting regulators of the three-enzyme ubiquitylation cascade are unknown. Here we report that the prenylated membrane-anchored ubiquitin-fold protein (MUB) is an early-acting regulator of subfamily-specific E2 activation. An AtMUB3:AtUBC8 co-crystal structure defines how MUBs inhibit E2∼Ub formation using a combination of E2 backside binding and a MUB-unique lap-bar loop to block E1 access. Since MUBs tether Arabidopsis group VI E2 enzymes (related to HsUbe2D and ScUbc4/5) to the plasma membrane, and inhibit E2 activation at physiological concentrations, they should function as potent plasma membrane localized regulators of Ub chain synthesis in eukaryotes. Our findings define a biochemical function for MUB, a family of highly conserved Ub-fold proteins, and provide an example of selective activation between cognate Ub E2s, previously thought to be constitutively activated by E1s.
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Registered trials
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.