scholarly journals Cell cycle-dependent regulation of SFK, JAK1 and STAT3 signaling by the protein tyrosine phosphatase TCPTP

Cell Cycle ◽  
2008 ◽  
Vol 7 (21) ◽  
pp. 3405-3416 ◽  
Author(s):  
Ben J. Shields ◽  
Naomi W. Court ◽  
Christine Hauser ◽  
Patricia E. Bukczynska ◽  
Tony Tiganis
Keyword(s):  
Cell Cycle ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Stat3 Signaling ◽  
Cycle Dependent

scholarly journals Functional Analysis of a Cell Cycle–Associated, Tumor-Suppressive Gene, Protein Tyrosine Phosphatase Receptor Type G, in Nasopharyngeal Carcinoma

2008 ◽  
Vol 68 (19) ◽  
pp. 8137-8145 ◽  
Author(s):  
Arthur Kwok Leung Cheung ◽  
Hong Lok Lung ◽  
Siu Chun Hung ◽  
Evan Wai Lok Law ◽  
Yue Cheng ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Functional Analysis ◽  
Nasopharyngeal Carcinoma ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
A Cell

scholarly journals Loss of Protein-tyrosine Phosphatase α (PTPα) Increases Proliferation and Delays Maturation of Oligodendrocyte Progenitor Cells

2012 ◽  
Vol 287 (15) ◽  
pp. 12529-12540 ◽  
Author(s):  
Pei-Shan Wang ◽  
Jing Wang ◽  
Yi Zheng ◽  
Catherine J. Pallen
Keyword(s):  
Cell Cycle ◽  
Progenitor Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Oligodendrocyte Progenitor Cells ◽  
Cell Cycle Exit ◽  
Oligodendrocyte Progenitor ◽  
Protein Tyrosine ◽  
Neural Stem Progenitor Cells

Tightly controlled termination of proliferation determines when oligodendrocyte progenitor cells (OPCs) can initiate differentiation and mature into myelin-forming cells. Protein-tyrosine phosphatase α (PTPα) promotes OPC differentiation, but its role in proliferation is unknown. Here we report that loss of PTPα enhanced in vitro proliferation and survival and decreased cell cycle exit and growth factor dependence of OPCs but not neural stem/progenitor cells. PTPα−/− mice have more oligodendrocyte lineage cells in embryonic forebrain and delayed OPC maturation. On the molecular level, PTPα-deficient mouse OPCs and rat CG4 cells have decreased Fyn and increased Ras, Cdc42, Rac1, and Rho activities, and reduced expression of the Cdk inhibitor p27Kip1. Moreover, Fyn was required to suppress Ras and Rho and for p27Kip1 accumulation, and Rho inhibition in PTPα-deficient cells restored expression of p27Kip1. We propose that PTPα-Fyn signaling negatively regulates OPC proliferation by down-regulating Ras and Rho, leading to p27Kip1 accumulation and cell cycle exit. Thus, PTPα acts in OPCs to limit self-renewal and facilitate differentiation.

scholarly journals Protein tyrosine phosphatase of liver regeneration-1 is required for normal timing of cell cycle progression during liver regeneration

2015 ◽  
Vol 308 (2) ◽  
pp. G85-G91 ◽  
Author(s):  
Yang Jiao ◽  
Diana Z. Ye ◽  
Zhaoyu Li ◽  
Monica Teta-Bissett ◽  
Yong Peng ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Liver Regeneration ◽  
Partial Hepatectomy ◽  
Protein Tyrosine Phosphatase ◽  
Cell Cycle Progression ◽  
Tyrosine Phosphatase ◽  
Mutant Mice ◽  
Cell Cycle Regulators ◽  
Cycle Progression ◽  
Protein Tyrosine

Protein tyrosine phosphatase of liver regeneration-1 ( Prl-1) is an immediate-early gene that is significantly induced during liver regeneration. Several in vitro studies have suggested that Prl-1 is important for the regulation of cell cycle progression. To evaluate its function in liver regeneration, we ablated the Prl-1 gene specifically in mouse hepatocytes using the Cre-loxP system. Prl-1 mutant mice ( Prl-1loxP/loxP;AlfpCre) appeared normal and fertile. Liver size and metabolic function in Prl-1 mutants were comparable to controls, indicating that Prl-1 is dispensable for liver development, postnatal growth, and hepatocyte differentiation. Mutant mice demonstrated a delay in DNA synthesis after 70% partial hepatectomy, although ultimate liver mass restoration was not affected. At 40 h posthepatectomy, reduced protein levels of the cell cycle regulators cyclin E, cyclin A2, cyclin B1, and cyclin-dependent kinase 1 were observed in Prl-1 mutant liver. Investigation of the major signaling pathways involved in liver regeneration demonstrated that phosphorylation of protein kinase B (AKT) and signal transducer and activator of transcription (STAT) 3 were significantly reduced at 40 h posthepatectomy in Prl-1 mutants. Taken together, this study provides evidence that Prl-1 is required for proper timing of liver regeneration after partial hepatectomy. Prl-1 promotes G1/S progression via modulating expression of several cell cycle regulators through activation of the AKT and STAT3 signaling pathway.

scholarly journals Knockdown of protein tyrosine phosphatase SHP-1 inhibits G1/S progression in prostate cancer cells through the regulation of components of the cell-cycle machinery

Oncogene ◽  
2009 ◽  
Vol 29 (3) ◽  
pp. 345-355 ◽  
Author(s):  
F J Rodríguez-Ubreva ◽  
A E Cariaga-Martinez ◽  
M A Cortés ◽  
M Romero-De Pablos ◽  
S Ropero ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Cycle ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Prostate Cancer Cells ◽  
Protein Tyrosine ◽  
Cell Cycle Machinery

scholarly journals Nuclear localization and cell cycle regulation of a murine protein tyrosine phosphatase.

1994 ◽  
Vol 14 (5) ◽  
pp. 3030-3040 ◽  
Author(s):  
U Tillmann ◽  
J Wagner ◽  
D Boerboom ◽  
H Westphal ◽  
M L Tremblay
Keyword(s):  
Cell Cycle ◽  
Nuclear Localization ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Protein ◽  
Nuclear Targeting ◽  
Protein Tyrosine ◽  
Nuclear Localization Signals ◽  
Human T Cell ◽  
Beta Galactosidase

MPTP is a murine homolog of the human T-cell protein tyrosine phosphatase (PTPase) and the rat PTP-S enzyme. Enzymatic activity of this ubiquitously expressed protein was demonstrated in immunoprecipitates from NIH 3T3 cells and in recombinant protein overexpressed in bacteria. Expression of beta-galactosidase-MPTP MPTP chimeric proteins in COS1 cells identified a nuclear localization signal at the carboxyl terminus of the MPTP that was sufficient to direct beta-galactosidase as well as a tagged version of the MPTP to the nucleus. Deletion analysis of amino acids within the nuclear targeting signal showed that this sequence does not conform to the bipartite type of nuclear localization signals. Furthermore, it was shown that the steady-state levels of MPTP RNA fluctuate in a cell cycle-specific manner. On the basis of these experiments, we discuss the possible function of MPTP in the cell cycle and other nuclear processes.

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