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PDBsum entry 3l6x
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Cell adhesion
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PDB id
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3l6x
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References listed in PDB file
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Key reference
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Title
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Dynamic and static interactions between p120 catenin and e-Cadherin regulate the stability of cell-Cell adhesion.
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Authors
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N.Ishiyama,
S.H.Lee,
S.Liu,
G.Y.Li,
M.J.Smith,
L.F.Reichardt,
M.Ikura.
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Ref.
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Cell, 2010,
141,
117-128.
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PubMed id
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Abstract
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The association of p120 catenin (p120) with the juxtamembrane domain (JMD) of
the cadherin cytoplasmic tail is critical for the surface stability of
cadherin-catenin cell-cell adhesion complexes. Here, we present the crystal
structure of p120 isoform 4A in complex with the JMD core region (JMD(core)) of
E-cadherin. The p120 armadillo repeat domain contains modular binding pockets
that are complementary to electrostatic and hydrophobic properties of the
JMD(core). Single-residue mutations within the JMD(core)-binding site of p120
abolished its interaction with E- and N-cadherins in vitro and in cultured
cells. These mutations of p120 enabled us to clearly differentiate between
N-cadherin-dependent and -independent steps of neuronal dendritic spine
morphogenesis crucial for synapse development. NMR studies revealed that p120
regulates the stability of cadherin-mediated cell-cell adhesion by associating
with the majority of the JMD, including residues implicated in clathrin-mediated
endocytosis and Hakai-dependent ubiquitination of E-cadherin, through its
discrete "dynamic" and "static" binding sites.
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