Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 31, Issue 21, Pages 4258-4269Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.05547-11
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Funding
- National Cancer Institute (Cancer Center) [5R01CA109035, 5 P50 CA127001-03, CA016672]
- Cancer Prevention and Research Institute of Texas [RP110252]
- American Cancer Society [RSG-09-277-01-CSM, RSG-08-288-01-GMC]
- The University of Texas MD Anderson Cancer Center
- Department of Defense [W81XWH-09-1-0349]
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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.
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