{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T23:01:46Z","timestamp":1791327706536,"version":"4.3.1"},"reference-count":60,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2006,6,5]],"date-time":"2006-06-05T00:00:00Z","timestamp":1149465600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Traffic"],"published-print":{"date-parts":[[2006,8]]},"abstract":"<jats:p><jats:bold>The endosomal sorting complex I required for transport (ESCRT\u2010I) is composed of the three subunits Vps23\/Tsg101, Vps28 and Vps37. ESCRT\u2010I is recruited to cellular membranes during multivesicular endosome biogenesis and by enveloped viruses such as HIV\u20101 to mediate budding from the cell. Here, we describe the crystal structure of a conserved C\u2010terminal domain from <jats:italic>Sacharomyces cerevisiae<\/jats:italic> Vps28 (Vps28\u2010CTD) at 3.05 \u00c5 resolution which folds independently into a four\u2010helical bundle structure. Co\u2010expression experiments of Vps28\u2010CTD, Vps23 and Vps37 suggest that Vps28\u2010CTD does not directly participate in ESCRT\u2010I assembly and may thus act as an adaptor module for downstream interaction partners. We show through mutagenesis studies that Vps28\u2010CTD employs its strictly conserved surface in the interaction with the ESCRT\u2010III factor Vps20. Furthermore, we present evidence that Vps28\u2010CTD is sufficient to rescue an equine infectious anaemia virus (EIAV) Gag late domain deletion. Vps28\u2010CTD mutations abolishing Vps20 interaction <jats:italic>in vitro<\/jats:italic> also prevent the rescue of the EIAV Gag late domain mutant consistent with a potential direct Vps28\u2010ESCRT\u2010III Vps20 recruitment. Therefore, the physiological relevant EIAV Gag\u2013Alix interaction can be functionally replaced by a Gag\u2010Vps28\u2010CTD fusion. Because both Alix and Vps28\u2010CTD can directly recruit ESCRT\u2010III proteins, ESCRT\u2010III assembly coupled to Vps4 action may therefore constitute the minimal budding machinery for EIAV release.<\/jats:bold><\/jats:p>","DOI":"10.1111\/j.1600-0854.2006.00440.x","type":"journal-article","created":{"date-parts":[[2006,6,6]],"date-time":"2006-06-06T11:01:54Z","timestamp":1149591714000},"page":"1007-1016","source":"Crossref","is-referenced-by-count":61,"title":["The Crystal Structure of the C\u2010Terminal Domain of Vps28 Reveals a Conserved Surface Required for Vps20 Recruitment"],"prefix":"10.1111","volume":"7","author":[{"given":"Estela","family":"Pineda\u2010Molina","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hassan","family":"Belrhali","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew 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