4r10
From Proteopedia
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| - | ''' | + | ==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo== |
| + | <StructureSection load='4r10' size='340' side='right' caption='[[4r10]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4r10]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R10 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4r0z|4r0z]], [[4r11|4r11]]</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=4r10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r10 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r10 RCSB], [http://www.ebi.ac.uk/pdbsum/4r10 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HMP2_CAEEL HMP2_CAEEL]] Required for cell migration during body enclosure and cell shape changes during body elongation.<ref>PMID:9531567</ref> [[http://www.uniprot.org/uniprot/HMR1_CAEEL HMR1_CAEEL]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Isoform A is required for cell migration during body enclosure and cell shape changes during body elongation. Required for proper localization of other junctional components, such as hmp-1, hmp-2 and jac-1. Isoform b is involved in axonal guidance in a subset of motor neurons.<ref>PMID:11790304</ref> <ref>PMID:12847081</ref> <ref>PMID:9531567</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In metazoan adherens junctions, beta-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein alpha-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for beta-catenin and promotes cell-cell adhesion in cell culture systems, but its importance has not been demonstrated in vivo. Here, we identify a critical phosphorylated serine in the C. elegans cadherin HMR-1 required for strong binding to the beta-catenin homolog HMP-2. Ablation of this phosphoserine interaction produces developmental defects that resemble full loss-of-function (Hammerhead and Humpback) phenotypes. Most metazoans possess a single gene for beta-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous beta-catenins; for example, C. elegans HMP-2 functions only in cell-cell adhesion, whereas SYS-1 mediates transcriptional activation through interactions with POP-1/Tcf. Our structural data define critical sequence differences responsible for the unique ligand specificities of these two proteins. | ||
| - | + | A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and beta-Catenin In Vitro and In Vivo.,Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI Dev Cell. 2015 Apr 6;33(1):82-93. doi: 10.1016/j.devcel.2015.02.005. PMID:25850673<ref>PMID:25850673</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Bang, I]] | ||
| + | [[Category: Choi, H J]] | ||
[[Category: Hardin, J]] | [[Category: Hardin, J]] | ||
[[Category: Loveless, T]] | [[Category: Loveless, T]] | ||
| - | [[Category: | + | [[Category: Lynch, A]] |
| - | [[Category: | + | [[Category: Weis, W I]] |
| - | [[Category: | + | [[Category: Armadillo repeat]] |
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Cell adhesion-protein binding complex]] | ||
| + | [[Category: Phosphorylation]] | ||
Revision as of 11:34, 30 April 2015
A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo
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