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PDBsum entry 4r11
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Cell adhesion/protein binding
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PDB id
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4r11
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Contents |
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534 a.a.
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43 a.a.
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508 a.a.
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38 a.a.
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References listed in PDB file
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Key reference
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Title
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A conserved phosphorylation switch controls the interaction between cadherin and β-Catenin in vitro and in vivo.
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Authors
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H.J.Choi,
T.Loveless,
A.M.Lynch,
I.Bang,
J.Hardin,
W.I.Weis.
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Ref.
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Dev Cell, 2015,
33,
82-93.
[DOI no: ]
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PubMed id
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Abstract
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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.
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