{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T09:51:25Z","timestamp":1791193885896,"version":"4.1.0"},"reference-count":36,"publisher":"Portland Press Ltd.","issue":"10","license":[{"start":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T00:00:00Z","timestamp":1790553600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100009613","name":"Universit\u00e4t Hohenheim","doi-asserted-by":"publisher","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}],"id":[{"id":"10.13039\/100009613","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,10,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>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 \u03b11 altered Mos10 localization, while the L150P mutation in helix \u03b14 abolished membrane association. A potential explanation for the effect of the L49P mutation on Mos10 function is suggested by AlphaFold modeling.<\/jats:p>","DOI":"10.1042\/bsr20260272","type":"journal-article","created":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T13:41:52Z","timestamp":1790602912000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Characterization of the Mos10 (Vps60) ESCRT-III complex"],"prefix":"10.1042","volume":"46","author":[{"given":"Jo\u00ebl","family":"Vollmar","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Lebensmittelwissenschaft und Biotechnologie, Fg. Hefegenetik und G\u00e4rungstechnologie, Universit\u00e4t Hohenheim, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Brune","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Lebensmittelwissenschaft und Biotechnologie, Fg. Hefegenetik und G\u00e4rungstechnologie, Universit\u00e4t Hohenheim, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8024-5686","authenticated-orcid":false,"given":"Ralf","family":"K\u00f6lling","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Lebensmittelwissenschaft und Biotechnologie, Fg. 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