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5y04

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Revision as of 07:42, 23 May 2018

Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin

Structural highlights

5y04 is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3w3r
Gene:	Vcl (LK3 transgenic mice), Ctnna1, Catna1 (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VINC_MOUSE] 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 (By similarity).[UniProtKB:P18206]^[1] [CTNA1_MOUSE] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.^[2]

Publication Abstract from PubMed

Mechanotransduction by alpha-catenin facilitates the force-dependent development of adherens junctions (AJs) by recruiting vinculin to reinforce actin anchoring of AJs. The alpha-catenin mechanotransducing action is facilitated by its force-sensing device region that autoinhibits the vinculin-binding site 1 (VBS1). Here, we report the high-resolution structure of the force-sensing device region of alpha-catenin, which shows the autoinhibited form comprised of helix bundles E, F and G. The cryptic VBS1 is embedded into helix bundle E stabilized by direct interactions with the autoinhibitory region forming helix bundles F and G. Our molecular dissection study showed that helix bundles F and G are stable in solution in each isolated form, whereas helix bundle E that contains VBS1 is unstable and intrinsically disordered in solution in the isolated form. We successfully identified key residues mediating the autoinhibition and produced mutated alpha-catenins that display variable force sensitivity and autoinhibition. Using these mutants, we demonstrate both in vitro and in vivo that, in the absence of this stabilization, the helix bundle containing VBS1 would adopt an unfolded form, thus exposing VBS for vinculin binding. We provide evidence for importance of mechanotransduction with the intrinsic force sensitivity for vinculin recruitment to adherens junctions of epithelial cell sheets with mutated alpha-catenins.

The force-sensing device region of alpha-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form.,Hirano Y, Amano Y, Yonemura S, Hakoshima T Genes Cells. 2018 Mar 15. doi: 10.1111/gtc.12578. PMID:29542234^[3]

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

References

↑ Coll JL, Ben-Ze'ev A, Ezzell RM, Rodriguez Fernandez JL, Baribault H, Oshima RG, Adamson ED. Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion. Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9161-5. PMID:7568093
↑ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell. 2005 Dec 2;123(5):903-15. PMID:16325583 doi:10.1016/j.cell.2005.09.021
↑ Hirano Y, Amano Y, Yonemura S, Hakoshima T. The force-sensing device region of alpha-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form. Genes Cells. 2018 Mar 15. doi: 10.1111/gtc.12578. PMID:29542234 doi:http://dx.doi.org/10.1111/gtc.12578

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/5y04"

@@ Line 3: / Line 3: @@
 <StructureSection load='5y04' size='340' side='right' caption='[[5y04]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5y04]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y04 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5y04]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y04 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w3r|3w3r]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vcl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Ctnna1, Catna1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5y04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y04 OCA], [http://pdbe.org/5y04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y04 RCSB], [http://www.ebi.ac.uk/pdbsum/5y04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y04 ProSAT]</span></td></tr>
 </table>
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5y04" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Catenin|Catenin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Lk3 transgenic mice]]
 [[Category: Hakoshima, T]]
 [[Category: Hirano, Y]]

5y04

From Proteopedia

Revision as of 07:42, 23 May 2018

Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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