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- Publisher Website: 10.1038/nsmb1163
- Scopus: eid_2-s2.0-33750592719
- PMID: 17057714
- WOS: WOS:000241817700018
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Article: Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain
Title | Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain |
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Authors | |
Issue Date | 2006 |
Citation | Nature Structural and Molecular Biology, 2006, v. 13, n. 11, p. 1031-1032 How to Cite? |
Abstract | ESCRT-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 Identifier | http://hdl.handle.net/10722/219528 |
ISSN | 2023 Impact Factor: 12.5 2023 SCImago Journal Rankings: 7.151 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Hirano, Satoshi | - |
dc.contributor.author | Suzuki, Nobuhiro | - |
dc.contributor.author | Slagsvold, Thomas | - |
dc.contributor.author | Kawasaki, Masato | - |
dc.contributor.author | Trambaiolo, Daniel | - |
dc.contributor.author | Kato, Ryuichi | - |
dc.contributor.author | Stenmark, Harald | - |
dc.contributor.author | Wakatsuki, Soichi | - |
dc.date.accessioned | 2015-09-23T02:57:18Z | - |
dc.date.available | 2015-09-23T02:57:18Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Nature Structural and Molecular Biology, 2006, v. 13, n. 11, p. 1031-1032 | - |
dc.identifier.issn | 1545-9993 | - |
dc.identifier.uri | http://hdl.handle.net/10722/219528 | - |
dc.description.abstract | ESCRT-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.language | eng | - |
dc.relation.ispartof | Nature Structural and Molecular Biology | - |
dc.title | Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1038/nsmb1163 | - |
dc.identifier.pmid | 17057714 | - |
dc.identifier.scopus | eid_2-s2.0-33750592719 | - |
dc.identifier.volume | 13 | - |
dc.identifier.issue | 11 | - |
dc.identifier.spage | 1031 | - |
dc.identifier.epage | 1032 | - |
dc.identifier.eissn | 1545-9985 | - |
dc.identifier.isi | WOS:000241817700018 | - |
dc.identifier.issnl | 1545-9985 | - |