PDBsum entry 4r11

Cell adhesion/protein binding

PDB id: 4r11

Contents

Protein chains

534 a.a.

43 a.a.

508 a.a.

38 a.a.

Metals

IOD ×9

Waters ×52

PDB id:

4r11

Name:

Cell adhesion/protein binding

Title:

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

Structure:

Protein humpback-2. Chain: a, c, e. Fragment: armadillo domain, unp residues 53-621. Engineered: yes. Cadherin-related hmr-1. Chain: b, d, f. Fragment: cytoplasmic domain, unp residues 2841-2920. Synonym: protein hammerhead. Engineered: yes

Source:

Caenorhabditis elegans. Roundworm. Organism_taxid: 6239. Gene: hmp-2, k05c4.6. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hmr-1, w02b9.1.

Resolution:

2.79Å R-factor: 0.203 R-free: 0.249

Authors:

H.-J.Choi,T.Loveless,A.Lynch,I.Bang,J.Hardin,W.I.Weis

Key ref:

H.J.Choi et al. (2015). A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. Dev Cell, 33, 82-93. PubMed id: 25850673 DOI: 10.1016/j.devcel.2015.02.005

Date:

03-Aug-14 Release date: 29-Apr-15

Protein chains

O44326  (HMP2_CAEEL) -  Beta-catenin-like protein hmp-2 from Caenorhabditis elegans

Seq: 678 a.a.

Struc: 534 a.a.

Protein chains

Q967F4  (HMR1_CAEEL) -  Cadherin-related hmr-1 from Caenorhabditis elegans

Seq: 2920 a.a.

Struc: 43 a.a.*

Protein chain

O44326  (HMP2_CAEEL) -  Beta-catenin-like protein hmp-2 from Caenorhabditis elegans

Seq: 678 a.a.

Struc: 508 a.a.

Protein chain

Q967F4  (HMR1_CAEEL) -  Cadherin-related hmr-1 from Caenorhabditis elegans

Seq: 2920 a.a.

Struc: 38 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1016/j.devcel.2015.02.005

Dev Cell 33:82-93 (2015)

PubMed id: 25850673

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

H.J.Choi, T.Loveless, A.M.Lynch, I.Bang, J.Hardin, W.I.Weis.

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.