ArticleThe Journal of cell biology2023
Vps60 initiates alternative ESCRT-III filaments.
Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Characterization of the Mos10 (Vps60) ESCRT-III complex.Bioscience reports · 2026Article
- Wbm0152, an outer membrane lipoprotein of the Wolbachia endosymbiont of Brugia malayi, inhibits yeast ESCRT complex activity.PLoS pathogens · 2025Article
- The evolution and mechanism of bacterial and archaeal ESCRT-III-like systems.Current opinion in structural biology · 2025Review
- The green ESCRTs: Newly defined roles for ESCRT proteins in plants.The Journal of biological chemistry · 2025Review
- Proteomic analysis across aged tissues reveals distinct signatures and the crucial involvement of midgut barrier function in the regulation of aging.Aging cell · 2025Article
- Exosome-Mediated Antigen Delivery: Unveiling Novel Strategies in Viral Infection Control and Vaccine Design.Vaccines · 2024Review
- Research progress of exosomes in the angiogenesis of digestive system tumour.Discover oncology · 2024Review
- ESCRT-III: a versatile membrane remodeling machinery and its implications in cellular processes and diseases.Animal cells and systems · 2024Review
- Dissecting membrane interfacial cellular processes: an in vitro reconstitution approach.The European physical journal. Special topics · 2024Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Endosomal sorting complex required for transport-III (ESCRT-III) participates in essential cellular functions, from cell division to endosome maturation. The remarkable increase of its subunit diversity through evolution may have enabled the acquisition of novel functions. Here, we characterize a novel ESCRT-III copolymer initiated by Vps60. Membrane-bound Vps60 polymers recruit Vps2, Vps24, Did2, and Ist1, as previously shown for Snf7. Snf7- and Vps60-based filaments can coexist on membranes without interacting as their polymerization and recruitment of downstream subunits remain spatially and biochemically separated. In fibroblasts, Vps60/CHMP5 and Snf7/CHMP4 are both recruited during endosomal functions and cytokinesis, but their localization is segregated and their recruitment dynamics are different. Contrary to Snf7/CHMP4, Vps60/CHMP5 is not recruited during nuclear envelope reformation. Taken together, our results show that Vps60 and Snf7 form functionally distinct ESCRT-III polymers, supporting the notion that diversification of ESCRT-III subunits through evolution is linked to the acquisition of new cellular functions.
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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.