p120 serine and threonine phosphorylation is controlled by multiple ligand-receptor pathways but not cadherin ligation.

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.

journal_name

Exp Cell Res

authors

Xia X,Carnahan RH,Vaughan MH,Wildenberg GA,Reynolds AB

doi

10.1016/j.yexcr.2006.07.007

subject

Has Abstract

pub_date

2006-10-15 00:00:00

pages

3336-48

issue

17

eissn

0014-4827

issn

1090-2422

pii

S0014-4827(06)00274-6

journal_volume

312

pub_type

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