| Structural highlights
3a58 is a 6 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| NonStd Res: | |
| Gene: | SEC3, PSL1, YER008C (ATCC 18824), RHO1, YPR165W, P9325.3 (ATCC 18824) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SEC3_YEAST] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. [RHO1_YEAST] Acts as a central regulator in the cell wall integrity signaling pathway, which is regulated by the cell cycle and in response to various types of cell wall stress. Integrates signals from different cell surface sensors, and activates a set of effectors, regulating processes including beta-glucan synthesis at the site of wall remodeling, gene expression related to cell wall biogenesis, organization of the actin cytoskeleton, and protein- and secretory vesicle-targeting to the growth site. Activates the protein kinase C (PKC1) MAP kinase cascade, the beta-1,3-glucan synthase (FKS1), the formin BNI1, the exocyst component SEC3 and the transcription factor SKN7.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The exocyst complex is a hetero-octameric protein complex that functions during cell polarization by tethering the secretory vesicle to the target membrane. The yeast exocyst subunit Sec3 binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P(2)) and the small GTPases Rho1 and Cdc42 via its N-terminal domain (Sec3-N), and these interactions target Sec3 to the plasma membrane. Here we report the crystal structure of the Sec3-N in complex with Rho1 at 2.6-A resolution. Sec3-N adopts a pleckstrin homology (PH) fold, despite having no detectable sequence homology with other PH domains of known structure. Clusters of conserved basic residues constitute a positively charged cleft, which was identified as a binding site for PtdIns(4,5)P(2). Residues Phe77, Ile115 and Leu131 of Sec3 bind to an extended hydrophobic surface formed around switch regions I and II of Rho1. To our knowledge, these are the first structural insights into how an exocyst subunit might interact with both protein and phospholipid factors on the target membrane.
Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3.,Yamashita M, Kurokawa K, Sato Y, Yamagata A, Mimura H, Yoshikawa A, Sato K, Nakano A, Fukai S Nat Struct Mol Biol. 2010 Feb;17(2):180-6. Epub 2010 Jan 10. PMID:20062059[16]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamochi W, Tanaka K, Nonaka H, Maeda A, Musha T, Takai Y. Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae. J Cell Biol. 1994 Jun;125(5):1077-93. PMID:8195291
- ↑ Wang T, Bretscher A. The rho-GAP encoded by BEM2 regulates cytoskeletal structure in budding yeast. Mol Biol Cell. 1995 Aug;6(8):1011-24. PMID:7579704
- ↑ Nonaka H, Tanaka K, Hirano H, Fujiwara T, Kohno H, Umikawa M, Mino A, Takai Y. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO J. 1995 Dec 1;14(23):5931-8. PMID:8846785
- ↑ Kohno H, Tanaka K, Mino A, Umikawa M, Imamura H, Fujiwara T, Fujita Y, Hotta K, Qadota H, Watanabe T, Ohya Y, Takai Y. Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 1996 Nov 15;15(22):6060-8. PMID:8947028
- ↑ Kamada Y, Qadota H, Python CP, Anraku Y, Ohya Y, Levin DE. Activation of yeast protein kinase C by Rho1 GTPase. J Biol Chem. 1996 Apr 19;271(16):9193-6. PMID:8621575
- ↑ Drgonova J, Drgon T, Tanaka K, Kollar R, Chen GC, Ford RA, Chan CS, Takai Y, Cabib E. Rho1p, a yeast protein at the interface between cell polarization and morphogenesis. Science. 1996 Apr 12;272(5259):277-9. PMID:8602514
- ↑ Qadota H, Python CP, Inoue SB, Arisawa M, Anraku Y, Zheng Y, Watanabe T, Levin DE, Ohya Y. Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-glucan synthase. Science. 1996 Apr 12;272(5259):279-81. PMID:8602515
- ↑ Guo W, Tamanoi F, Novick P. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat Cell Biol. 2001 Apr;3(4):353-60. PMID:11283608 doi:10.1038/35070029
- ↑ Watanabe D, Abe M, Ohya Y. Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-beta-glucan synthesis. Yeast. 2001 Jul;18(10):943-51. PMID:11447600 doi:10.1002/yea.742
- ↑ Tolliday N, VerPlank L, Li R. Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis. Curr Biol. 2002 Oct 29;12(21):1864-70. PMID:12419188
- ↑ Schmidt A, Schmelzle T, Hall MN. The RHO1-GAPs SAC7, BEM2 and BAG7 control distinct RHO1 functions in Saccharomyces cerevisiae. Mol Microbiol. 2002 Sep;45(5):1433-41. PMID:12207708
- ↑ Dong Y, Pruyne D, Bretscher A. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. J Cell Biol. 2003 Jun 23;161(6):1081-92. Epub 2003 Jun 16. PMID:12810699 doi:10.1083/jcb.200212040
- ↑ Valdivia RH, Schekman R. The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane. Proc Natl Acad Sci U S A. 2003 Sep 2;100(18):10287-92. Epub 2003 Aug 19. PMID:12928491 doi:http://dx.doi.org/10.1073/pnas.1834246100
- ↑ Fitch PG, Gammie AE, Lee DJ, de Candal VB, Rose MD. Lrg1p Is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Genetics. 2004 Oct;168(2):733-46. PMID:15514049 doi:10.1534/genetics.104.028027
- ↑ Marelli M, Smith JJ, Jung S, Yi E, Nesvizhskii AI, Christmas RH, Saleem RA, Tam YY, Fagarasanu A, Goodlett DR, Aebersold R, Rachubinski RA, Aitchison JD. Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane. J Cell Biol. 2004 Dec 20;167(6):1099-112. Epub 2004 Dec 13. PMID:15596542 doi:10.1083/jcb.200404119
- ↑ Yamashita M, Kurokawa K, Sato Y, Yamagata A, Mimura H, Yoshikawa A, Sato K, Nakano A, Fukai S. Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3. Nat Struct Mol Biol. 2010 Feb;17(2):180-6. Epub 2010 Jan 10. PMID:20062059 doi:10.1038/nsmb.1722
|
