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Article: Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain

TitleEap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain
Authors
Issue Date2005
Citation
Journal of Biological Chemistry, 2005, v. 280, n. 20, p. 19600-19606 How to Cite?
AbstractUbiquitination serves as a key sorting signal in the lysosomal degradation of endocytosed receptors through the ability of ubiquitinated membrane proteins to be recognized and sorted by ubiquitin-binding proteins along the endocytic route. The ESCRT-II complex in yeast contains one such protein, Vps36, which harbors a ubiquitin-binding NZF domain and is required for vacuolar sorting of ubiquitinated membrane proteins. Surprisingly, the presumptive mammalian ortholog Eap45 lacks the ubiquitin-binding module of Vps36, and it is thus not clear whether mammalian ESCRT-II functions to bind ubiquitinated cargo. In this paper, we provide evidence that Eap45 contains a novel ubiquitin-binding domain, GLUE (GRAM-like ubiquitin-binding in Eap45), which binds ubiquitin with similar affinity and specificity as other ubiquitin-binding domains. The GLUE domain shares similarities in its primary and predicted secondary structures to phosphoinositide-binding GRAM and PH domains. Accordingly, we find that Eap45 binds to a subset of 3-phosphoinositides, suggesting that ubiquitin recognition could be coordinated with phosphoinositide binding. Furthermore, we show that Eap45 colocalizes with ubiquitinated proteins on late endosomes. These results are consistent with a role for Eap45 in endosomal sorting of ubiquitinated cargo. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/219487
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151

 

DC FieldValueLanguage
dc.contributor.authorSlagsvold, Thomas-
dc.contributor.authorAasland, Rein-
dc.contributor.authorHirano, Satoshi-
dc.contributor.authorBache, Kristi G.-
dc.contributor.authorRaiborg, Camilla-
dc.contributor.authorTrambaiolo, Daniel-
dc.contributor.authorWakatsuki, Soichi-
dc.contributor.authorStenmark, Harald-
dc.date.accessioned2015-09-23T02:57:12Z-
dc.date.available2015-09-23T02:57:12Z-
dc.date.issued2005-
dc.identifier.citationJournal of Biological Chemistry, 2005, v. 280, n. 20, p. 19600-19606-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/219487-
dc.description.abstractUbiquitination serves as a key sorting signal in the lysosomal degradation of endocytosed receptors through the ability of ubiquitinated membrane proteins to be recognized and sorted by ubiquitin-binding proteins along the endocytic route. The ESCRT-II complex in yeast contains one such protein, Vps36, which harbors a ubiquitin-binding NZF domain and is required for vacuolar sorting of ubiquitinated membrane proteins. Surprisingly, the presumptive mammalian ortholog Eap45 lacks the ubiquitin-binding module of Vps36, and it is thus not clear whether mammalian ESCRT-II functions to bind ubiquitinated cargo. In this paper, we provide evidence that Eap45 contains a novel ubiquitin-binding domain, GLUE (GRAM-like ubiquitin-binding in Eap45), which binds ubiquitin with similar affinity and specificity as other ubiquitin-binding domains. The GLUE domain shares similarities in its primary and predicted secondary structures to phosphoinositide-binding GRAM and PH domains. Accordingly, we find that Eap45 binds to a subset of 3-phosphoinositides, suggesting that ubiquitin recognition could be coordinated with phosphoinositide binding. Furthermore, we show that Eap45 colocalizes with ubiquitinated proteins on late endosomes. These results are consistent with a role for Eap45 in endosomal sorting of ubiquitinated cargo. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.titleEap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.M501510200-
dc.identifier.pmid15755741-
dc.identifier.scopuseid_2-s2.0-19944419643-
dc.identifier.volume280-
dc.identifier.issue20-
dc.identifier.spage19600-
dc.identifier.epage19606-

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