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| | ==STRUCTURE OF YEAST ENT1 ENTH DOMAIN== | | ==STRUCTURE OF YEAST ENT1 ENTH DOMAIN== |
| - | <StructureSection load='5loz' size='340' side='right' caption='[[5loz]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='5loz' size='340' side='right'caption='[[5loz]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5loz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5loz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hoa|1hoa]], [[1edu|1edu]], [[1eyh|1eyh]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loz OCA], [http://pdbe.org/5loz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5loz RCSB], [http://www.ebi.ac.uk/pdbsum/5loz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5loz ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loz OCA], [https://pdbe.org/5loz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5loz RCSB], [https://www.ebi.ac.uk/pdbsum/5loz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5loz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ENT1_YEAST ENT1_YEAST]] Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.<ref>PMID:10449404</ref> <ref>PMID:11694597</ref> <ref>PMID:12529323</ref> | + | [https://www.uniprot.org/uniprot/ENT1_YEAST ENT1_YEAST] Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.<ref>PMID:10449404</ref> <ref>PMID:11694597</ref> <ref>PMID:12529323</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5loz" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5loz" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Epsin|Epsin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Prag, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Tanner, N]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Alpha-alpha superhelix]] | + | [[Category: Prag G]] |
| - | [[Category: Clathrin]] | + | [[Category: Tanner N]] |
| - | [[Category: Endocytosis adaptor]]
| + | |
| - | [[Category: Eps15]]
| + | |
| - | [[Category: Lipid]]
| + | |
| - | [[Category: Ubiquitin]]
| + | |
| - | [[Category: Ubiquitin receptor]]
| + | |
| - | [[Category: Ubiquitin-binding domain]]
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| Structural highlights
Function
ENT1_YEAST Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.[1] [2] [3]
Publication Abstract from PubMed
About one-third of the eukaryotic proteome undergoes ubiquitylation, but the enzymatic cascades leading to substrate modification are largely unknown. We present a genetic selection tool that utilizes Escherichia coli, which lack deubiquitylases, to identify interactions along ubiquitylation cascades. Coexpression of split antibiotic resistance protein tethered to ubiquitin and ubiquitylation target together with a functional ubiquitylation apparatus results in a covalent assembly of the resistance protein, giving rise to bacterial growth on selective media. We applied the selection system to uncover an E3 ligase from the pathogenic bacteria EHEC and to identify the epsin ENTH domain as an ultraweak ubiquitin-binding domain. The latter was complemented with a structure-function analysis of the ENTH-ubiquitin interface. We also constructed and screened a yeast fusion library, discovering Sem1 as a novel ubiquitylation substrate of Rsp5 E3 ligase. Collectively, our selection system provides a robust high-throughput approach for genetic studies of ubiquitylation cascades and for small-molecule modulator screening.
A bacterial genetic selection system for ubiquitylation cascade discovery.,Levin-Kravets O, Tanner N, Shohat N, Attali I, Keren-Kaplan T, Shusterman A, Artzi S, Varvak A, Reshef Y, Shi X, Zucker O, Baram T, Katina C, Pilzer I, Ben-Aroya S, Prag G Nat Methods. 2016 Oct 3. doi: 10.1038/nmeth.4003. PMID:27694912[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wendland B, Steece KE, Emr SD. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 1999 Aug 16;18(16):4383-93. PMID:10449404 doi:10.1093/emboj/18.16.4383
- ↑ Watson HA, Cope MJ, Groen AC, Drubin DG, Wendland B. In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol Biol Cell. 2001 Nov;12(11):3668-79. PMID:11694597
- ↑ Aguilar RC, Watson HA, Wendland B. The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J Biol Chem. 2003 Mar 21;278(12):10737-43. Epub 2003 Jan 14. PMID:12529323 doi:http://dx.doi.org/10.1074/jbc.M211622200
- ↑ Levin-Kravets O, Tanner N, Shohat N, Attali I, Keren-Kaplan T, Shusterman A, Artzi S, Varvak A, Reshef Y, Shi X, Zucker O, Baram T, Katina C, Pilzer I, Ben-Aroya S, Prag G. A bacterial genetic selection system for ubiquitylation cascade discovery. Nat Methods. 2016 Oct 3. doi: 10.1038/nmeth.4003. PMID:27694912 doi:http://dx.doi.org/10.1038/nmeth.4003
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