{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,7]],"date-time":"2026-11-07T22:31:10Z","timestamp":1794090670143,"version":"4.8.0"},"reference-count":40,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2011,12,6]],"date-time":"2011-12-06T00:00:00Z","timestamp":1323129600000},"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":[[2012,2]]},"abstract":"<jats:p>Dynamins are a conserved family of proteins involved in many membrane fusion and fission events. Previously, the dynamin\u2010related protein <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 was shown to localize to endocytic sites, and yeast carrying deletions for genes encoding both the <jats:styled-content style=\"fixed-case\">BAR<\/jats:styled-content> domain protein <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 and <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 had a more severe endocytic scission defect than either deletion alone. <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 and <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 localize to endocytic sites at the onset of invagination and disassemble concomitant with inward vesicle movement. <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167\u2010<jats:styled-content style=\"fixed-case\">GFP<\/jats:styled-content> localization is reduced in cells lacking <jats:italic>vps1<\/jats:italic> suggesting that <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 influences <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 association with the endocytic complex. Unlike classical dynamins, <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 does not have a proline\u2013arginine domain that could interact with <jats:styled-content style=\"fixed-case\">SH<\/jats:styled-content>3 domain\u2010containing proteins. Thus, while <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 has an <jats:styled-content style=\"fixed-case\">SH<\/jats:styled-content>3 domain, it is not clear how an interaction would be mediated. Here, we demonstrate an interaction between <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 <jats:styled-content style=\"fixed-case\">SH<\/jats:styled-content>3 domain and the single type <jats:styled-content style=\"fixed-case\">I<\/jats:styled-content> <jats:styled-content style=\"fixed-case\">SH<\/jats:styled-content>3\u2010binding motif in <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1. Mutant <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 that cannot bind <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 rescues all membrane fusion\/fission functions associated with <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 except for endocytic function, demonstrating the specificity and mechanistic importance of the interaction. <jats:italic>In vitro<\/jats:italic>, an <jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>161\/<jats:styled-content style=\"fixed-case\">Rvs<\/jats:styled-content>167 heterodimer can disassemble <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 oligomers. Overall, the data support the idea that <jats:styled-content style=\"fixed-case\">Vps<\/jats:styled-content>1 and the amphiphysins function together to mediate scission during endocytosis in yeast.<\/jats:p>","DOI":"10.1111\/j.1600-0854.2011.01311.x","type":"journal-article","created":{"date-parts":[[2011,11,14]],"date-time":"2011-11-14T16:31:44Z","timestamp":1321288304000},"page":"317-328","source":"Crossref","is-referenced-by-count":46,"title":["Yeast Dynamin <scp>Vps<\/scp>1 and Amphiphysin <scp>Rvs<\/scp>167 Function Together During Endocytosis"],"prefix":"10.1111","volume":"13","author":[{"given":"Iwona I.","family":"Smaczynska\u2010de Rooij","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Biotechnology Firth Court Western Bank University of Sheffield  Sheffield S10 2TN UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ellen G.","family":"Allwood","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biotechnology Firth Court Western Bank University of Sheffield  Sheffield S10 2TN UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ritu","family":"Mishra","sequence":"additional","affiliation":[{"name":"School of Biological and Biomedical Sciences Durham University  Durham DH1 3LE UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wesley I.","family":"Booth","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biotechnology Firth Court Western Bank University of Sheffield  Sheffield S10 2TN UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Soheil","family":"Aghamohammadzadeh","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biotechnology Firth Court Western Bank University of Sheffield  Sheffield S10 2TN UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin W.","family":"Goldberg","sequence":"additional","affiliation":[{"name":"School of 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