4r0z: Difference between revisions
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==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo== | |||
<StructureSection load='4r0z' size='340' side='right'caption='[[4r0z]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4r0z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R0Z FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.005Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0z OCA], [https://pdbe.org/4r0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r0z RCSB], [https://www.ebi.ac.uk/pdbsum/4r0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0z ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | |||
<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> | |||
<div class="pdbe-citations 4r0z" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | |||
[[Category: Large Structures]] | |||
[[Category: Bang I]] | |||
[[Category: Choi H-J]] | |||
[[Category: Hardin J]] | |||
[[Category: Loveless T]] | |||
[[Category: Lynch A]] | |||
[[Category: Weis WI]] | |||
