3dyt: Difference between revisions

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<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=3dyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dyt RCSB], [http://www.ebi.ac.uk/pdbsum/3dyt PDBsum]</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=3dyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dyt RCSB], [http://www.ebi.ac.uk/pdbsum/3dyt PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SNX9_HUMAN SNX9_HUMAN]] May be involved in several stages of intracellular trafficking. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate.<ref>PMID:11799118</ref> <ref>PMID:12952949</ref> <ref>PMID:15703209</ref> <ref>PMID:17609109</ref> <ref>PMID:18388313</ref> <ref>PMID:20427313</ref> <ref>PMID:21048941</ref> <ref>PMID:17948057</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 01:56, 25 December 2014

Crystal structure of Snx9PX-BAR (230-595), C2221Crystal structure of Snx9PX-BAR (230-595), C2221

Structural highlights

3dyt is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:SNX9, SH3PX1, SH3PXD3A (Homo sapiens)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[SNX9_HUMAN] May be involved in several stages of intracellular trafficking. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate.[1] [2] [3] [4] [5] [6] [7] [8]

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

Endophilin and Sorting Nexin 9 (Snx9) play key roles in endocytosis by membrane curvature sensing and remodeling via their Bin/Amphiphysin/Rvs (BAR) domains. BAR and the related F-BAR domains form dimeric, crescent-shaped units that occur N- or C-terminally to other lipid-binding, adaptor, or catalytic modules. In crystal structures, the PX-BAR unit of Snx9 (Snx9(PX-BAR)) adopts an overall compact, moderately curved conformation. SAXS-based solution studies revealed an alternative, more curved state of Snx9(PX-BAR) in which the PX domains are flexibly connected to the BAR domains, providing a model for how Snx9 exhibits lipid-dependent curvature preferences. In contrast, Endophilin appears to be rigid in solution, and the SH3 domains are located at the distal tips of a BAR domain dimer with fixed curvature. We also observed tip-to-tip interactions between the BAR domains in a trigonal crystal form of Snx9(PX-BAR) reminiscent of functionally important interactions described for F-BAR domains.

Structure and plasticity of Endophilin and Sorting Nexin 9.,Wang Q, Kaan HY, Hooda RN, Goh SL, Sondermann H Structure. 2008 Oct 8;16(10):1574-87. PMID:18940612[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Lin Q, Lo CG, Cerione RA, Yang W. The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. J Biol Chem. 2002 Mar 22;277(12):10134-8. Epub 2002 Jan 17. PMID:11799118 doi:http://dx.doi.org/10.1074/jbc.M110329200
  2. ↑ Lundmark R, Carlsson SR. Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components. J Biol Chem. 2003 Nov 21;278(47):46772-81. Epub 2003 Sep 2. PMID:12952949 doi:http://dx.doi.org/10.1074/jbc.M307334200
  3. ↑ Soulet F, Yarar D, Leonard M, Schmid SL. SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis. Mol Biol Cell. 2005 Apr;16(4):2058-67. Epub 2005 Feb 9. PMID:15703209 doi:http://dx.doi.org/10.1091/mbc.E04-11-1016
  4. ↑ Yarar D, Waterman-Storer CM, Schmid SL. SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Dev Cell. 2007 Jul;13(1):43-56. PMID:17609109 doi:http://dx.doi.org/10.1016/j.devcel.2007.04.014
  5. ↑ Shin N, Ahn N, Chang-Ileto B, Park J, Takei K, Ahn SG, Kim SA, Di Paolo G, Chang S. SNX9 regulates tubular invagination of the plasma membrane through interaction with actin cytoskeleton and dynamin 2. J Cell Sci. 2008 Apr 15;121(Pt 8):1252-63. doi: 10.1242/jcs.016709. PMID:18388313 doi:http://dx.doi.org/10.1242/jcs.016709
  6. ↑ Park J, Kim Y, Lee S, Park JJ, Park ZY, Sun W, Kim H, Chang S. SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane. J Cell Sci. 2010 May 15;123(Pt 10):1742-50. doi: 10.1242/jcs.064170. Epub 2010, Apr 27. PMID:20427313 doi:http://dx.doi.org/10.1242/jcs.064170
  7. ↑ Wang JT, Kerr MC, Karunaratne S, Jeanes A, Yap AS, Teasdale RD. The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome formation by SNX-PX-BAR proteins. PLoS One. 2010 Oct 29;5(10):e13763. doi: 10.1371/journal.pone.0013763. PMID:21048941 doi:10.1371/journal.pone.0013763
  8. ↑ Pylypenko O, Lundmark R, Rasmuson E, Carlsson SR, Rak A. The PX-BAR membrane-remodeling unit of sorting nexin 9. EMBO J. 2007 Nov 14;26(22):4788-800. Epub 2007 Oct 18. PMID:17948057
  9. ↑ Wang Q, Kaan HY, Hooda RN, Goh SL, Sondermann H. Structure and plasticity of Endophilin and Sorting Nexin 9. Structure. 2008 Oct 8;16(10):1574-87. PMID:18940612 doi:10.1016/j.str.2008.07.016

3dyt, resolution 2.08Å

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