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Protein tyrosine phosphatase, non-receptor type 12

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may regulate protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of the oncogene c-ABL and thus may play a role in oncogenesis. This PTP was also shown to interact with, and dephosphorylate, various products related to cytoskeletal structure and cell adhesion, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin. This suggests it has a regulatory role in controlling cell shape and mobility. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Oct 2008] (from NCBI)
Papers using PTP-PEST antibodies
Inducible rodent models of acquired podocyte diseases
Takano Tomoko et al., In Journal of Signal Transduction, 2008
... Antibodies were purchased from the following sources: PTP1B and SHP2 (BD Biosciences), PTP-PEST (Cell Signaling), ...
Papers on PTP-PEST
Tyrosine-protein phosphatase nonreceptor type 12 is a novel prognostic biomarker for esophageal squamous cell carcinoma.
Wen et al., Guangzhou, China. In Ann Thorac Surg, 2012
High expression of PTPN12 is associated with favorable disease free survival in esophageal squamous cell carcinoma patients.
Dynamin and PTP-PEST cooperatively regulate Pyk2 dephosphorylation in osteoclasts.
Bruzzaniti et al., Indianapolis, United States. In Int J Biochem Cell Biol, 2012
the dephosphorylation of Pyk2 requires dynamin's GTPase activity and is mediated by the tyrosine phosphatase PTP-PEST.
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.
Lu et al., Houston, United States. In Mol Cell Biol, 2011
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
Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase.
Westbrook et al., Houston, United States. In Cell, 2011
Using a genetic screen, study identifies the PTPN12 tyrosine phosphatase as a tumor suppressor in
Tyrosine phosphatases in the HER2-directed motility of ovarian cancer cells: Involvement of PTPN12, ERK5 and FAK.
Villa-Moruzzi, Pisa, Italy. In Anal Cell Pathol (amst), 2010
Suggest PTPN12 and ERK5 mediate HER2-driven cell motility in ovarian cancer cells, through FAK targeting.
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