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| | <StructureSection load='4tu3' size='340' side='right'caption='[[4tu3]], [[Resolution|resolution]] 3.19Å' scene=''> | | <StructureSection load='4tu3' size='340' side='right'caption='[[4tu3]], [[Resolution|resolution]] 3.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tu3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TU3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tu3]] is a 2 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=4TU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TU3 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAC1, RSD1, YKL212W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), VPS74, YDR372C, D9481.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 3.187Å</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=4tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu3 OCA], [http://pdbe.org/4tu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4tu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tu3 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=4tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tu3 OCA], [https://pdbe.org/4tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tu3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SAC1_YEAST SAC1_YEAST]] Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton.<ref>PMID:10625610</ref> <ref>PMID:11514624</ref> [[http://www.uniprot.org/uniprot/VPS74_YEAST VPS74_YEAST]] Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting.<ref>PMID:20026658</ref> <ref>PMID:22889169</ref> <ref>PMID:18410729</ref> | + | [https://www.uniprot.org/uniprot/SAC1_YEAST SAC1_YEAST] Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton.<ref>PMID:10625610</ref> <ref>PMID:11514624</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | + | *[[Dual specificity phosphatase 3D structures|Dual specificity phosphatase 3D structures]] |
| | *[[Phosphoinositide phosphatase|Phosphoinositide phosphatase]] | | *[[Phosphoinositide phosphatase|Phosphoinositide phosphatase]] |
| - | *[[Vacuolar protein sorting-associated protein|Vacuolar protein sorting-associated protein]] | + | *[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cai, Y]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Horenkamp, F A]] | + | [[Category: Cai Y]] |
| - | [[Category: Reinisch, K R]] | + | [[Category: Horenkamp FA]] |
| - | [[Category: Golgi apparatus]] | + | [[Category: Reinisch KR]] |
| - | [[Category: Hydrolase-protein transport complex]]
| + | |
| - | [[Category: Phosphatidylinositol phosphate]]
| + | |
| - | [[Category: Phosphoric monoester hydrolase]]
| + | |
| - | [[Category: Protein complex]]
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| Structural highlights
Function
SAC1_YEAST Phosphoinositide phosphatase that hydrolyzes PtdIns(3)P and PtdIns(4)P. Has low activity towards PtdIns(3,5)P2. May be involved in the coordination of the activities of the secretory pathway and the actin cytoskeleton.[1] [2]
Publication Abstract from PubMed
Sac1 is a phosphoinositide phosphatase of the endoplasmic reticulum and Golgi apparatus that controls organelle membrane composition principally via regulation of phosphatidylinositol 4-phosphate signaling. We present a characterization of the structure of the N-terminal portion of yeast Sac1, containing the conserved Sac1 homology domain, in complex with Vps74, a phosphatidylinositol 4-kinase effector and the orthologue of human GOLPH3. The interface involves the N-terminal subdomain of the Sac1 homology domain, within which mutations in the related Sac3/Fig4 phosphatase have been linked to Charcot-Marie-Tooth disorder CMT4J and amyotrophic lateral sclerosis. Disruption of the Sac1-Vps74 interface results in a broader distribution of phosphatidylinositol 4-phosphate within the Golgi apparatus and failure to maintain residence of a medial Golgi mannosyltransferase. The analysis prompts a revision of the membrane-docking mechanism for GOLPH3 family proteins and reveals how an effector of phosphoinositide signaling serves a dual function in signal termination.
Sac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus.,Cai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG J Cell Biol. 2014 Aug 18;206(4):485-91. doi: 10.1083/jcb.201404041. Epub 2014 Aug, 11. PMID:25113029[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hughes WE, Woscholski R, Cooke FT, Patrick RS, Dove SK, McDonald NQ, Parker PJ. SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases. J Biol Chem. 2000 Jan 14;275(2):801-8. PMID:10625610
- ↑ Foti M, Audhya A, Emr SD. Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol Biol Cell. 2001 Aug;12(8):2396-411. PMID:11514624
- ↑ Cai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG. Sac1-Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. J Cell Biol. 2014 Aug 18;206(4):485-91. doi: 10.1083/jcb.201404041. Epub 2014 Aug, 11. PMID:25113029 doi:http://dx.doi.org/10.1083/jcb.201404041
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