# Characterization of the Mos10 (Vps60) ESCRT-III complex

Article · Vollmar J, Brune T, Kölling R

- Archive id: doi:10.1042/bsr20260272
- Published: 2026-10-01
- Venue: Bioscience reports
- DOI: https://doi.org/10.1042/bsr20260272
- PMID: 42803658
- PMCID: PMC13643019
- Citations: 0
- Source URL: https://doi.org/10.1042/bsr20260272
- PDF: https://europepmc.org/articles/PMC13643019/pdf
- Provenance: europepmc

## Abstract

The endosomal sorting complex required for transport (ESCRT)-III protein Mos10 (also known as Vps60) forms an alternative ESCRT-III complex in yeast. Here, we explored the relationship between the Mos10 complex and the classical Snf7-based complex. Both proteins could in principle form completely independent complexes or mixed complexes. To address the present issue, we examined the composition of ESCRT-III in different mutants of the endosomal protein sorting pathway by co-immunoprecipitation. We found that the formation of the Mos10 complex was dependent on the activity of the AAA+ ATPase Vps4. At the same time, loss of Vps4 activity led to an accumulation of the canonical ESCRT-III proteins Snf7, Vps2, and Vps24. In none of the mutants tested could a complex be detected that contains only Mos10 and no Snf7. We therefore favor the view that Snf7 and Mos10 form mixed complexes, which could play a role in the disassembly of ESCRT-III. To further dissect the interactions among the ESCRT-III subunits, Mos10 mutants were isolated. The L49P mutation in helix α1 altered Mos10 localization, while the L150P mutation in helix α4 abolished membrane association. A potential explanation for the effect of the L49P mutation on Mos10 function is suggested by AlphaFold modeling.

_Abstract reproduced under CC-BY (article license as recorded by Europe PMC; abstract reproduced unmodified apart from markup removal)._

Topics: [AI Protein Design & Structure Prediction](https://space-kitty.com/topics/protein-design)

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