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3zdl

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Revision as of 14:37, 25 December 2014

Vinculin head (1-258) in complex with a RIAM fragment

Structural highlights

3zdl is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[VINC_CHICK] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.^[1] ^[2] ^[3] [AB1IP_HUMAN] Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.^[4] ^[5]

Publication Abstract from PubMed

Talin activates integrins, couples them to F-actin and recruits vinculin to focal adhesions (FAs). Here we report the structural characterization of the talin rod, 13 helical bundles (R1-R13) organized into a compact cluster of 4-helix bundles (R2-R4) within a linear chain of 5-helix bundles. Nine of the bundles contain vinculin-binding sites (VBSs) - R2R3 are atypical each containing two VBSs. Talin R2R3 also binds synergistically to RIAM, a Rap1 effector involved in integrin activation. Biochemical and structural data show that vinculin and RIAM binding to R2R3 is mutually exclusive. Moreover, vinculin binding requires domain unfolding while RIAM binds the folded R2R3 double domain. In cells, RIAM is enriched in nascent adhesions at the leading edge whereas vinculin is enriched in FAs, and expression of the talin-binding domain of vinculin displaces RIAM from FAs. We propose a model in which RIAM binding to R2R3 initially recruits talin to membranes where it activates integrins. As talin engages F-actin, force exerted on R2R3 disrupts RIAM binding and exposes the VBSs, which recruit vinculin to stabilize the complex.

RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover.,Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, Elliott PR, Roberts GC, Ballestrem C, Critchley DR, Barsukov IL J Biol Chem. 2013 Feb 6. PMID:23389036^[6]

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

References

↑ Zhang Z, Izaguirre G, Lin SY, Lee HY, Schaefer E, Haimovich B. The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading. Mol Biol Cell. 2004 Sep;15(9):4234-47. Epub 2004 Jun 30. PMID:15229287 doi:10.1091/mbc.E04-03-0264
↑ le Duc Q, Shi Q, Blonk I, Sonnenberg A, Wang N, Leckband D, de Rooij J. Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol. 2010 Jun 28;189(7):1107-15. doi: 10.1083/jcb.201001149. PMID:20584916 doi:10.1083/jcb.201001149
↑ Peng X, Cuff LE, Lawton CD, DeMali KA. Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin. J Cell Sci. 2010 Feb 15;123(Pt 4):567-77. doi: 10.1242/jcs.056432. Epub 2010 Jan , 19. PMID:20086044 doi:10.1242/jcs.056432
↑ Inagaki T, Suzuki S, Miyamoto T, Takeda T, Yamashita K, Komatsu A, Yamauchi K, Hashizume K. The retinoic acid-responsive proline-rich protein is identified in promyeloleukemic HL-60 cells. J Biol Chem. 2003 Dec 19;278(51):51685-92. Epub 2003 Oct 6. PMID:14530287 doi:10.1074/jbc.M308016200
↑ Lafuente EM, van Puijenbroek AA, Krause M, Carman CV, Freeman GJ, Berezovskaya A, Constantine E, Springer TA, Gertler FB, Boussiotis VA. RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. Dev Cell. 2004 Oct;7(4):585-95. PMID:15469846 doi:10.1016/j.devcel.2004.07.021
↑ Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, Elliott PR, Roberts GC, Ballestrem C, Critchley DR, Barsukov IL. RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover. J Biol Chem. 2013 Feb 6. PMID:23389036 doi:http://dx.doi.org/10.1074/jbc.M112.438119

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zdl"

@@ Line 5: / Line 5: @@
 </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=3zdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zdl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zdl RCSB], [http://www.ebi.ac.uk/pdbsum/3zdl PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/VINC_CHICK VINC_CHICK]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.<ref>PMID:15229287</ref> <ref>PMID:20584916</ref> <ref>PMID:20086044</ref>  [[http://www.uniprot.org/uniprot/AB1IP_HUMAN AB1IP_HUMAN]] Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.<ref>PMID:14530287</ref> <ref>PMID:15469846</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3zdl

From Proteopedia

Revision as of 14:37, 25 December 2014

Vinculin head (1-258) in complex with a RIAM fragment

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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