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Article: Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain

TitleStructural basis of ubiquitin recognition by mammalian Eap45 GLUE domain
Authors
Hirano, SatoshiSuzuki, NobuhiroSlagsvold, ThomasKawasaki, MasatoTrambaiolo, DanielKato, RyuichiStenmark, HaraldWakatsuki, Soichi
Issue Date2006
Citation
Nature Structural and Molecular Biology, 2006, v. 13, n. 11, p. 1031-1032 How to Cite?
DOI: http://dx.doi.org/10.1038/nsmb1163
AbstractESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE-Ub complex structure, Ub binds far from the proposed PI-binding site of Eap45 GLUE, suggesting their independent binding. © 2006 Nature Publishing Group.
Persistent Identifierhttp://hdl.handle.net/10722/219528
ISSN
1545-9993
2021 Impact Factor: 18.361
2020 SCImago Journal Rankings: 9.448
ISI Accession Number ID
WOS:000241817700018

 

DC FieldValueLanguage
dc.contributor.authorHirano, Satoshi-
dc.contributor.authorSuzuki, Nobuhiro-
dc.contributor.authorSlagsvold, Thomas-
dc.contributor.authorKawasaki, Masato-
dc.contributor.authorTrambaiolo, Daniel-
dc.contributor.authorKato, Ryuichi-
dc.contributor.authorStenmark, Harald-
dc.contributor.authorWakatsuki, Soichi-
dc.date.accessioned2015-09-23T02:57:18Z-
dc.date.available2015-09-23T02:57:18Z-
dc.date.issued2006-
dc.identifier.citationNature Structural and Molecular Biology, 2006, v. 13, n. 11, p. 1031-1032-
dc.identifier.issn1545-9993-
dc.identifier.urihttp://hdl.handle.net/10722/219528-
dc.description.abstractESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE-Ub complex structure, Ub binds far from the proposed PI-binding site of Eap45 GLUE, suggesting their independent binding. © 2006 Nature Publishing Group.-
dc.languageeng-
dc.relation.ispartofNature Structural and Molecular Biology-
dc.titleStructural basis of ubiquitin recognition by mammalian Eap45 GLUE domain-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/nsmb1163-
dc.identifier.pmid17057714-
dc.identifier.scopuseid_2-s2.0-33750592719-
dc.identifier.volume13-
dc.identifier.issue11-
dc.identifier.spage1031-
dc.identifier.epage1032-
dc.identifier.eissn1545-9985-
dc.identifier.isiWOS:000241817700018-
dc.identifier.issnl1545-9985-

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