5cmw
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ENT5_YEAST ENT5_YEAST]] Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).<ref>PMID:12483220</ref> <ref>PMID:15107463</ref> | [[http://www.uniprot.org/uniprot/ENT5_YEAST ENT5_YEAST]] Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).<ref>PMID:12483220</ref> <ref>PMID:15107463</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Clathrin-coated vesicles (CCVs) play critical roles in multiple cellular processes, including nutrient uptake, endosome/lysosome biogenesis, pathogen invasion, regulation of signalling receptors, etc. Saccharomyces cerevisiae Ent5 (ScEnt5) is one of the two major adaptors supporting the CCV-mediated TGN/endosome traffic in yeast cells. However, the classification and phosphoinositide binding characteristic of ScEnt5 remain elusive. Here we report the crystal structures of the ScEnt5 N-terminal domain, and find that ScEnt5 contains an insertion alpha' helix that does not exist in other ENTH or ANTH domains. Furthermore, we investigate the classification of ScEnt5-N(31-191) by evolutionary history analyses and structure comparisons, and find that the ScEnt5 N-terminal domain shows different phosphoinositide binding property from rEpsin1 and rCALM. Above results facilitate the understanding of the ScEnt5-mediated vesicle coat formation process. | ||
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| + | Structural and functional insight into the N-terminal domain of the clathrin adaptor Ent5 from Saccharomyces cerevisiae.,Zhang F, Song Y, Ebrahimi M, Niu L, Teng M, Li X Biochem Biophys Res Commun. 2016 Sep 2;477(4):786-93. doi:, 10.1016/j.bbrc.2016.06.136. Epub 2016 Jun 28. PMID:27369074<ref>PMID:27369074</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5cmw" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:19, 5 October 2016
Crystal structure of yeast Ent5 N-terminal domain-soaked in KI
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