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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)
Top mentioned proteins: paxillin, Src, Pts, V1a, focal adhesion kinase
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
PTP-PEST controls EphA3 activation and ephrin-induced cytoskeletal remodelling.
Lackmann et al., Australia. In J Cell Sci, Feb 2016
PTP-PEST (also known as PTPN12) is a central regulator of actin cytoskeletal dynamics.
Genomic profiling of invasive melanoma cell lines by array comparative genomic hybridization.
Balázs et al., Debrecen, Hungary. In Melanoma Res, Jan 2016
Invasive primary cell lines showed high frequencies of CNAs, including the loss of 7q and gain of 12q chromosomal regions targeting PTPN12, ADAM22, FZD1, TFPI2, GNG11, COL1A2, SMURF1, VGF, RELN and GLIPR1 genes.
Loss of PTPN12 Stimulates Progression of ErbB2-Dependent Breast Cancer by Enhancing Cell Survival, Migration, and Epithelial-to-Mesenchymal Transition.
Veillette et al., Montréal, Canada. In Mol Cell Biol, Jan 2016
PTPN12 is a cytoplasmic protein tyrosine phosphatase (PTP) reported to be a tumor suppressor in breast cancer, through its capacity to dephosphorylate oncogenic receptor protein tyrosine kinases (PTKs), such as ErbB2.
Mosaic partial deletion of PTPN12 in a child with interrupted aortic arch type A.
Schimmenti et al., Montréal, Canada. In Am J Med Genet A, Nov 2015
The goal of this study was to identify the significance of a de novo mosaic PTPN12 partial deletion identified in a newborn with an interrupted aortic arch type A, ventricular septal defect, and pyloric stenosis.
MVP-Associated Filamin A Mutations Affect FlnA-PTPN12 (PTP-PEST) Interactions.
Mérot et al., Nantes, France. In J Cardiovasc Dev Dis, Oct 2015
Here, using the first repeats (1-8) of FlnA as a bait in a yeast two-hybrid screen, we identified the tyrosine phosphatase PTPN12 (PTP-PEST) as a specific binding partner of this region of FlnA protein.
Decreased expression of protein tyrosine phosphatase non-receptor type 12 is involved in the proliferation and recurrence of bladder transitional cell carcinoma.
Wu et al., Yanji, China. In Oncol Lett, Sep 2015
UNASSIGNED: Protein tyrosine phosphatase non-receptor type 12 (PTPN12) has been shown to be involved in the development of a number of types of carcinoma.
Protein tyrosine phosphatase nonreceptor type 12 suppresses the proliferation of renal cell carcinoma by inhibiting the activity of the PI3K/mTOR pathway.
Jin et al., Yanji, China. In J Buon, Sep 2015
PURPOSE: To determine the expression and functions of protein tyrosine phosphatase nonreceptor type 12 (PTPN12) in renal cell carcinoma (RCC).
[Regulation on EGFR function via its interacting proteins and its potential application].
He et al., In Sheng Li Ke Xue Jin Zhan, 2013
For the multiple EGFR interaction proteins, B1R enhances Erk/MAPK signaling, while PTPN12, Kek1, CEACAM1 and NHERF repress Erk/MAPK signaling.
Regulation of tumor cell migration by protein tyrosine phosphatase (PTP)-proline-, glutamate-, serine-,and threonine-rich sequence (PEST).
Lu et al., Houston, United States. In Ai Zheng, 2013
PTP-PEST activity can be regulated transcriptionally via gene deletion or mutation in several types of human cancers or via post-translational modifications, including phosphorylation, oxidation, and caspase-dependent cleavage.
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.
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.
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
Uncovering a tumor suppressor for triple-negative breast cancers.
Brugge et al., Boston, United States. In Cell, 2011
Now Sun et al. (2011) find that the activity of the protein tyrosine phosphatase PTPN12 is lost in a large percentage of this breast cancer subtype, offering molecular drivers and possible therapeutic targets for this heterogeneous and intractable cancer.
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.
The phosphatase PTP-PEST promotes secondary T cell responses by dephosphorylating the protein tyrosine kinase Pyk2.
Veillette et al., Montréal, Canada. In Immunity, 2010
PTP-PEST controls Pyk2 activity and is a positive regulator of secondary T cell activation.
ArgBP2 and the SoHo family of adapter proteins in oncogenic diseases.
Soubeyran et al., Marseille, France. In Cell Adh Migr, 2009
We could show that part of the molecular mechanism involved the interaction of ArgBP2 with the Arp2/3 activator WAVE1, the tyrosine phosphatase PTP-PEST, and the tyrosine kinase c-Abl.
PEST family phosphatases in immunity, autoimmunity, and autoinflammatory disorders.
Davidson et al., Montréal, Canada. In Immunol Rev, 2009
The proline-, glutamic acid-, serine- and threonine-rich (PEST) family of protein tyrosine phosphatases (PTPs) includes proline-enriched phosphatase (PEP)/lymphoid tyrosine phosphatase (LYP), PTP-PEST, and PTP-hematopoietic stem cell fraction (HSCF).
Protein tyrosine phosphatases in osteoclast differentiation, adhesion, and bone resorption.
Elson et al., Israel. In Eur J Cell Biol, 2008
Here we summarize available information concerning the known and hypothesized roles of the best-researched PTPs in osteoclasts - PTPRO, PTP epsilon, SHP-1, and PTP-PEST.
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