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Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domainStructural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain
Structural highlights
Function[VPS36_HUMAN] Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into vesicles that accumulate within multivesicular bodies (MVBs). Crystallographic and biochemical analyses reveal that the GLUE domain of the human ESCRT-II EAP45 (also called VPS36) subunit is a split pleckstrin-homology domain that binds ubiquitin along one edge of the beta-sandwich. The structure suggests how human ESCRT-II can couple recognition of ubiquitinated cargoes and endosomal phospholipids during MVB protein sorting. Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain.,Alam SL, Langelier C, Whitby FG, Koirala S, Robinson H, Hill CP, Sundquist WI Nat Struct Mol Biol. 2006 Nov;13(11):1029-30. Epub 2006 Oct 22. PMID:17057716[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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