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| | <StructureSection load='4cz2' size='340' side='right'caption='[[4cz2]], [[Resolution|resolution]] 2.97Å' scene=''> | | <StructureSection load='4cz2' size='340' side='right'caption='[[4cz2]], [[Resolution|resolution]] 2.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cz2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CZ2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cz2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CZ2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.97Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cym|4cym]]</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=4cz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cz2 OCA], [https://pdbe.org/4cz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cz2 RCSB], [https://www.ebi.ac.uk/pdbsum/4cz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cz2 ProSAT]</span></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=4cz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cz2 OCA], [http://pdbe.org/4cz2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cz2 RCSB], [http://www.ebi.ac.uk/pdbsum/4cz2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cz2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RAB32_HUMAN RAB32_HUMAN]] Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.<ref>PMID:12186851</ref> <ref>PMID:21255211</ref> [[http://www.uniprot.org/uniprot/ANR27_HUMAN ANR27_HUMAN]] May be a Rab21 guanine exchange factor and regulate endosome dynamics (By similarity). | + | [https://www.uniprot.org/uniprot/RAB32_HUMAN RAB32_HUMAN] Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.<ref>PMID:12186851</ref> <ref>PMID:21255211</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 4cz2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4cz2" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ankyrin repeat domain-containing protein 3D structures|Ankyrin repeat domain-containing protein 3D structures]] |
| | + | *[[Ras-related protein Rab 3D structures|Ras-related protein Rab 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Evans, P R]] | + | [[Category: Evans PR]] |
| - | [[Category: McCoy, A J]] | + | [[Category: McCoy AJ]] |
| - | [[Category: Owen, D J]] | + | [[Category: Owen DJ]] |
| - | [[Category: Perez-Dorado, I]] | + | [[Category: Perez-Dorado I]] |
| - | [[Category: Schaefer, I B]] | + | [[Category: Schaefer IB]] |
| - | [[Category: Endosome]]
| + | |
| - | [[Category: Melanosome biogenesis]]
| + | |
| - | [[Category: Rab]]
| + | |
| - | [[Category: Rab-effector]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Varp]]
| + | |
| - | [[Category: Vesicle trafficking]]
| + | |
| Structural highlights
Function
RAB32_HUMAN Acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.[1] [2]
Publication Abstract from PubMed
VARP is a Rab32/38 effector that also binds to the endosomal/lysosomal R-SNARE VAMP7. VARP binding regulates VAMP7 participation in SNARE complex formation and can therefore influence VAMP7-mediated membrane fusion events. Mutant versions of VARP that cannot bind Rab32:GTP, designed on the basis of the VARP ankyrin repeat/Rab32:GTP complex structure described here, unexpectedly retain endosomal localization, showing that VARP recruitment is not dependent on Rab32 binding. We show that recruitment of VARP to the endosomal membrane is mediated by its direct interaction with VPS29, a subunit of the retromer complex, which is involved in trafficking from endosomes to the TGN and the cell surface. Transport of GLUT1 from endosomes to the cell surface requires VARP, VPS29, and VAMP7 and depends on the direct interaction between VPS29 and VARP. Finally, we propose that endocytic cycling of VAMP7 depends on its interaction with VARP and, consequently, also on retromer.
VARP Is Recruited on to Endosomes by Direct Interaction with Retromer, Where Together They Function in Export to the Cell Surface.,Hesketh GG, Perez-Dorado I, Jackson LP, Wartosch L, Schafer IB, Gray SR, McCoy AJ, Zeldin OB, Garman EF, Harbour ME, Evans PR, Seaman MN, Luzio JP, Owen DJ Dev Cell. 2014 May 21. pii: S1534-5807(14)00230-5. doi:, 10.1016/j.devcel.2014.04.010. PMID:24856514[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Alto NM, Soderling J, Scott JD. Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics. J Cell Biol. 2002 Aug 19;158(4):659-68. Epub 2002 Aug 19. PMID:12186851 doi:http://dx.doi.org/10.1083/jcb.200204081
- ↑ Seto S, Tsujimura K, Koide Y. Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic. 2011 Apr;12(4):407-20. doi: 10.1111/j.1600-0854.2011.01165.x. Epub 2011 , Feb 21. PMID:21255211 doi:10.1111/j.1600-0854.2011.01165.x
- ↑ Hesketh GG, Perez-Dorado I, Jackson LP, Wartosch L, Schafer IB, Gray SR, McCoy AJ, Zeldin OB, Garman EF, Harbour ME, Evans PR, Seaman MN, Luzio JP, Owen DJ. VARP Is Recruited on to Endosomes by Direct Interaction with Retromer, Where Together They Function in Export to the Cell Surface. Dev Cell. 2014 May 21. pii: S1534-5807(14)00230-5. doi:, 10.1016/j.devcel.2014.04.010. PMID:24856514 doi:http://dx.doi.org/10.1016/j.devcel.2014.04.010
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