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4r11

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Revision as of 18:34, 1 February 2017

A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo

Structural highlights

4r11 is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:	,
Related:	4r0z, 4r10
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HMP2_CAEEL] Required for cell migration during body enclosure and cell shape changes during body elongation.^[1] [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.^[2] ^[3] ^[4]

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^[5]

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

References

↑ Costa M, Raich W, Agbunag C, Leung B, Hardin J, Priess JR. A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo. J Cell Biol. 1998 Apr 6;141(1):297-308. PMID:9531567
↑ Broadbent ID, Pettitt J. The C. elegans hmr-1 gene can encode a neuronal classic cadherin involved in the regulation of axon fasciculation. Curr Biol. 2002 Jan 8;12(1):59-63. PMID:11790304
↑ Pettitt J, Cox EA, Broadbent ID, Flett A, Hardin J. The Caenorhabditis elegans p120 catenin homologue, JAC-1, modulates cadherin-catenin function during epidermal morphogenesis. J Cell Biol. 2003 Jul 7;162(1):15-22. PMID:12847081 doi:http://dx.doi.org/10.1083/jcb.200212136
↑ Costa M, Raich W, Agbunag C, Leung B, Hardin J, Priess JR. A putative catenin-cadherin system mediates morphogenesis of the Caenorhabditis elegans embryo. J Cell Biol. 1998 Apr 6;141(1):297-308. PMID:9531567
↑ Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and beta-Catenin In Vitro and In Vivo. Dev Cell. 2015 Apr 6;33(1):82-93. doi: 10.1016/j.devcel.2015.02.005. PMID:25850673 doi:http://dx.doi.org/10.1016/j.devcel.2015.02.005

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4r11"

@@ Line 1: / Line 1: @@
 ==A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo==
 <StructureSection load='4r11' size='340' side='right' caption='[[4r11]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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]], [[4r10|4r10]]</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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum]</span></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=4r11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r11 OCA], [http://pdbe.org/4r11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r11 RCSB], [http://www.ebi.ac.uk/pdbsum/4r11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r11 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4r11" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4r11

From Proteopedia

Revision as of 18:34, 1 February 2017

A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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