p120 serine and threonine phosphorylation is controlled by multiple ligand-receptor pathways but not cadherin ligation.
Exp Cell Res
; 312(17): 3336-48, 2006 Oct 15.
Article
en En
| MEDLINE
| ID: mdl-16935280
ABSTRACT
p120-catenin (p120) regulates cadherin turnover and is required for cadherin stability. Extensive and dynamic phosphorylation on tyrosine, serine and threonine residues in the N-terminal regulatory domain has been postulated to regulate p120 function, possibly through modulation of the efficiency of p120/cadherin interaction. Here we have utilized novel phospho-specific monoclonal antibodies to four major p120 serine and threonine phosphorylation sites to monitor individual phosphorylation events and their consequences. Surprisingly, membrane-localization and not cadherin interaction is the main determinant in p120 serine and threonine phosphorylation and dephosphorylation. Furthermore, the phospho-status of these four residues had no obvious effect on p120's role in cadherin complex stabilization or cell-cell adhesion. Interestingly, dephosphorylation was dramatically induced by PKC activation, but PKC-independent pathways were also evident. The data suggest that p120 dephosphorylation at these sites is modulated by multiple cell surface receptors primarily through PKC-dependent pathways, but these changes do not seem to reduce p120/cadherin affinity.
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Bases de datos:
MEDLINE
Asunto principal:
Fosfoproteínas
/
Serina
/
Treonina
/
Cadherinas
/
Moléculas de Adhesión Celular
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Exp Cell Res
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos