| First Author | Xia X | Year | 2006 |
| Journal | Exp Cell Res | Volume | 312 |
| Issue | 17 | Pages | 3336-48 |
| PubMed ID | 16935280 | Mgi Jnum | J:114378 |
| Mgi Id | MGI:3688935 | Doi | 10.1016/j.yexcr.2006.07.007 |
| Citation | Xia X, et al. (2006) p120 serine and threonine phosphorylation is controlled by multiple ligand-receptor pathways but not cadherin ligation. Exp Cell Res 312(17):3336-48 |
| abstractText | 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. |
