| http://purl.uniprot.org/citations/22586082 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22586082 | http://www.w3.org/2000/01/rdf-schema#comment | "αE-catenin, an essential component of the adherens junction, interacts with the classical cadherin-β-catenin complex and with F-actin, but its precise role is unknown. αE-catenin also binds to the F-actin-binding protein vinculin, which also appears to be important in junction assembly. Vinculin and αE-catenin are homologs that contain a series of helical bundle domains, D1-D5. We mapped the vinculin-binding site to a sequence in D3a comprising the central two helices of a four-helix bundle. The crystal structure of this peptide motif bound to vinculin D1 shows that the two helices adopt a parallel, colinear arrangement suggesting that the αE-catenin D3a bundle must unfold in order to bind vinculin. We show that αE-catenin D3 binds strongly to vinculin, whereas larger fragments and full-length αE-catenin bind approximately 1,000-fold more weakly. Thus, intramolecular interactions within αE-catenin inhibit binding to vinculin. The actin-binding activity of vinculin is inhibited by an intramolecular interaction between the head (D1-D4) and the actin-binding D5 tail. In the absence of F-actin, there is no detectable binding of αE-catenin D3 to full-length vinculin; however, αE-catenin D3 promotes binding of vinculin to F-actin whereas full-length αE-catenin does not. These findings support the combinatorial or "coincidence" model of activation in which binding of high-affinity proteins to the vinculin head and tail is required to shift the conformational equilibrium of vinculin from a closed, autoinhibited state to an open, stable F-actin-binding state. The data also imply that αE-catenin must be activated in order to bind to vinculin."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1203906109"xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Bankston L.A."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Choi H.J."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Liddington R.C."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Pokutta S."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Weis W.I."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Cadwell G.W."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/author | "Bobkov A.A."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/pages | "8576-8581"xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/title | "alphaE-catenin is an autoinhibited molecule that coactivates vinculin."xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://purl.uniprot.org/core/volume | "109"xsd:string |
| http://purl.uniprot.org/citations/22586082 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22586082 |
| http://purl.uniprot.org/citations/22586082 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/22586082 |
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