4R0Z
A conserved phosphorylation switch controls the interaction between cadherin and beta-catenin in vitro and in vivo
Summary for 4R0Z
| Entry DOI | 10.2210/pdb4r0z/pdb |
| Related | 4R10 4R11 |
| Descriptor | Protein humpback-2, FORMIC ACID (3 entities in total) |
| Functional Keywords | armadillo repeat, cell adhesion |
| Biological source | Caenorhabditis elegans (roundworm) |
| Cellular location | Cell junction, adherens junction : O44326 |
| Total number of polymer chains | 1 |
| Total formula weight | 69104.70 |
| Authors | Choi, H.-J.,Loveless, T.,Lynch, A.,Bang, I.,Hardin, J.,Weis, W.I. (deposition date: 2014-08-03, release date: 2015-04-29, Last modification date: 2023-11-08) |
| Primary citation | Choi, H.J.,Loveless, T.,Lynch, A.M.,Bang, I.,Hardin, J.,Weis, W.I. A Conserved Phosphorylation Switch Controls the Interaction between Cadherin and beta-Catenin In Vitro and In Vivo Dev.Cell, 33:82-93, 2015 Cited by PubMed Abstract: In metazoan adherens junctions, β-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein α-catenin. Phosphorylation of a Ser/Thr-rich region in the cadherin tail dramatically enhances affinity for β-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 β-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 β-catenin, which is also a transcriptional coactivator in Wnt signaling. Nematodes and planaria, however, have a set of paralogous β-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. PubMed: 25850673DOI: 10.1016/j.devcel.2015.02.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.005 Å) |
Structure validation
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