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- Publisher Website: 10.1074/jbc.M501510200
- Scopus: eid_2-s2.0-19944419643
- PMID: 15755741
- WOS: WOS:000229113700023
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Article: Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain
Title | Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain |
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Authors | |
Issue Date | 2005 |
Citation | Journal of Biological Chemistry, 2005, v. 280, n. 20, p. 19600-19606 How to Cite? |
Abstract | Ubiquitination 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 Identifier | http://hdl.handle.net/10722/219487 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Slagsvold, Thomas | - |
dc.contributor.author | Aasland, Rein | - |
dc.contributor.author | Hirano, Satoshi | - |
dc.contributor.author | Bache, Kristi G. | - |
dc.contributor.author | Raiborg, Camilla | - |
dc.contributor.author | Trambaiolo, Daniel | - |
dc.contributor.author | Wakatsuki, Soichi | - |
dc.contributor.author | Stenmark, Harald | - |
dc.date.accessioned | 2015-09-23T02:57:12Z | - |
dc.date.available | 2015-09-23T02:57:12Z | - |
dc.date.issued | 2005 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2005, v. 280, n. 20, p. 19600-19606 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10722/219487 | - |
dc.description.abstract | Ubiquitination 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.language | eng | - |
dc.relation.ispartof | Journal of Biological Chemistry | - |
dc.title | Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide- interacting GLUE domain | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1074/jbc.M501510200 | - |
dc.identifier.pmid | 15755741 | - |
dc.identifier.scopus | eid_2-s2.0-19944419643 | - |
dc.identifier.volume | 280 | - |
dc.identifier.issue | 20 | - |
dc.identifier.spage | 19600 | - |
dc.identifier.epage | 19606 | - |
dc.identifier.isi | WOS:000229113700023 | - |
dc.identifier.issnl | 0021-9258 | - |