Abstract
p120 catenin is a scaffold protein that interacts with cadherin cytoplasmic domain and acts as a crucial component of the signalling that regulates the cycle of adherens junction formation and disassembly. Here, we review the nature of stimuli that modulate p120ctn function and are translated as serine/threonine and tyrosine phosphorylation events at this multisite substrate for a variety of protein kinases. We also highlight recent findings that tentatively link phosphorylation of p120ctn to its role as a signal integrator capable to influence the state of the cadherin adhesive bond, the cytoskeleton and cell motility.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Animals
-
Cadherins / metabolism
-
Catenins
-
Cell Adhesion
-
Cell Adhesion Molecules / chemistry
-
Cell Adhesion Molecules / metabolism*
-
Cell Movement
-
Cytoskeleton / metabolism
-
Delta Catenin
-
Humans
-
Models, Biological
-
Phosphoproteins / chemistry
-
Phosphoproteins / metabolism*
-
Phosphorylation
-
Protein Serine-Threonine Kinases / metabolism
-
Protein Tyrosine Phosphatases / chemistry
-
Protein Tyrosine Phosphatases / metabolism
-
Protein-Tyrosine Kinases / metabolism
Substances
-
Cadherins
-
Catenins
-
Cell Adhesion Molecules
-
Phosphoproteins
-
Protein-Tyrosine Kinases
-
Protein Serine-Threonine Kinases
-
Protein Tyrosine Phosphatases
-
Delta Catenin
-
CTNND1 protein, human