| First Author | Zheng Y | Year | 2011 |
| Journal | Mol Cell Biol | Volume | 31 |
| Issue | 21 | Pages | 4258-69 |
| PubMed ID | 21876001 | Mgi Jnum | J:178339 |
| Mgi Id | MGI:5298162 | Doi | 10.1128/MCB.05547-11 |
| Citation | Zheng Y, et al. (2011) Ras-induced and extracellular signal-regulated kinase 1 and 2 phosphorylation-dependent isomerization of protein tyrosine phosphatase (PTP)-PEST by PIN1 promotes FAK dephosphorylation by PTP-PEST. Mol Cell Biol 31(21):4258-69 |
| abstractText | Protein tyrosine phosphatase (PTP)-PEST is a critical regulator of cell adhesion and migration. However, the mechanism by which PTP-PEST is regulated in response to oncogenic signaling to dephosphorylate its substrates remains unclear. Here, we demonstrate that activated Ras induces extracellular signal-regulated kinase 1 and 2-dependent phosphorylation of PTP-PEST at S571, which recruits PIN1 to bind to PTP-PEST. Isomerization of the phosphorylated PTP-PEST by PIN1 increases the interaction between PTP-PEST and FAK, which leads to the dephosphorylation of FAK Y397 and the promotion of migration, invasion, and metastasis of v-H-Ras-transformed cells. These findings uncover an important mechanism for the regulation of PTP-PEST in activated Ras-induced tumor progression. |
