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| | ==Identification of yeast R-SNARE Nyv1p as a novel longin domain protein== | | ==Identification of yeast R-SNARE Nyv1p as a novel longin domain protein== |
| - | <StructureSection load='2fz0' size='340' side='right'caption='[[2fz0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2fz0' size='340' side='right'caption='[[2fz0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fz0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FZ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fz0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FZ0 FirstGlance]. <br> |
| - | </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=2fz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fz0 OCA], [http://pdbe.org/2fz0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fz0 RCSB], [http://www.ebi.ac.uk/pdbsum/2fz0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fz0 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2fz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fz0 OCA], [https://pdbe.org/2fz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fz0 RCSB], [https://www.ebi.ac.uk/pdbsum/2fz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fz0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NYV1_YEAST NYV1_YEAST]] Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step.<ref>PMID:10385523</ref> <ref>PMID:11080502</ref> <ref>PMID:14734531</ref> <ref>PMID:9144293</ref> | + | [https://www.uniprot.org/uniprot/NYV1_YEAST NYV1_YEAST] Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step.<ref>PMID:10385523</ref> <ref>PMID:11080502</ref> <ref>PMID:14734531</ref> <ref>PMID:9144293</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Wen, W]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Zhang, M]] | + | [[Category: Wen W]] |
| - | [[Category: Longin domain]] | + | [[Category: Zhang M]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Snare protein]]
| + | |
| Structural highlights
Function
NYV1_YEAST Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step.[1] [2] [3] [4]
Publication Abstract from PubMed
Using nuclear magnetic resonance spectroscopy, we establish that the N-terminal domain of the yeast vacuolar R-SNARE Nyv1p adopts a longin-like fold similar to those of Sec22b and Ykt6p. Nyv1p is sorted to the limiting membrane of the vacuole via the adaptor protein (AP)3 adaptin pathway, and we show that its longin domain is sufficient to direct transport to this location. In contrast, we found that the longin domains of Sec22p and Ykt6p were not sufficient to direct their localization. A YXX phi-like adaptin-dependent sorting signal (Y31GTI34) unique to the longin domain of Nyv1p mediates interactions with the AP3 complex in vivo and in vitro. We show that amino acid substitutions to Y31GTI34 (Y31Q;I34Q) resulted in mislocalization of Nyv1p as well as reduced binding of the mutant protein to the AP3 complex. Although the sorting of Nyv1p to the limiting membrane of the vacuole is dependent upon the Y31GTI34 motif, and Y31 in particular, our findings with structure-based amino acid substitutions in the mu chain (Apm3p) of yeast AP3 suggest a mechanistically distinct role for this subunit in the recognition of YXX phi-like sorting signals.
Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein.,Wen W, Chen L, Wu H, Sun X, Zhang M, Banfield DK Mol Biol Cell. 2006 Oct;17(10):4282-99. Epub 2006 Jul 19. PMID:16855025[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ungermann C, von Mollard GF, Jensen ON, Margolis N, Stevens TH, Wickner W. Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. J Cell Biol. 1999 Jun 28;145(7):1435-42. PMID:10385523
- ↑ Takita Y, Engstrom L, Ungermann C, Cunningham KW. Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. J Biol Chem. 2001 Mar 2;276(9):6200-6. Epub 2000 Nov 15. PMID:11080502 doi:http://dx.doi.org/10.1074/jbc.M009191200
- ↑ Merz AJ, Wickner WT. Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen. J Cell Biol. 2004 Jan 19;164(2):195-206. PMID:14734531 doi:http://dx.doi.org/10.1083/jcb.200310105
- ↑ Nichols BJ, Ungermann C, Pelham HR, Wickner WT, Haas A. Homotypic vacuolar fusion mediated by t- and v-SNAREs. Nature. 1997 May 8;387(6629):199-202. PMID:9144293 doi:http://dx.doi.org/10.1038/387199a0
- ↑ Wen W, Chen L, Wu H, Sun X, Zhang M, Banfield DK. Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein. Mol Biol Cell. 2006 Oct;17(10):4282-99. Epub 2006 Jul 19. PMID:16855025 doi:http://dx.doi.org/E06-02-0128
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