scholarly journals The prognostic value of Cyclin-Dependent Kinase 5 and Protein Phosphatase 2A in Gastric Cancer

2018 ◽  
Vol 9 (23) ◽  
pp. 4404-4412 ◽  
Author(s):  
Jian-Xian Lin ◽  
Xin-Sheng Xie ◽  
Xiong-Feng Weng ◽  
Chao-Hui Zheng ◽  
Jian-Wei Xie ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Protein Phosphatase ◽  
Prognostic Value ◽  
Protein Phosphatase 2A ◽  
Cyclin Dependent Kinase ◽  
Phosphatase 2A ◽  
Cyclin Dependent Kinase 5

Neuronal Cyclin-Dependent Kinase-5 Phosphorylation Sites in Neurofilament Protein (NF-H) Are Dephosphorylated by Protein Phosphatase 2A

2002 ◽  
Vol 64 (6) ◽  
pp. 2681-2690 ◽  
Author(s):  
Veeranna ◽  
K. T. Shetty ◽  
W. T. Link ◽  
H. Jaffe ◽  
J. Wang ◽  
...  
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Phosphorylation Sites ◽  
Cyclin Dependent Kinase ◽  
Neurofilament Protein ◽  
Phosphatase 2A ◽  
Cyclin Dependent Kinase 5

scholarly journals Loss of a Protein Phosphatase 2A Regulatory Subunit (Cdc55p) Elicits Improper Regulation of Swe1p Degradation

2000 ◽  
Vol 20 (21) ◽  
pp. 8143-8156 ◽  
Author(s):  
Haifeng Yang ◽  
Wei Jiang ◽  
Matthew Gentry ◽  
Richard L. Hallberg
Keyword(s):  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Cell Types ◽  
Regulatory Subunit ◽  
Cyclin Dependent Kinase ◽  
Wild Type ◽  
Phosphatase 2A

ABSTRACT CDC55 encodes a Saccharomyces cerevisiaeprotein phosphatase 2A (PP2A) regulatory subunit.cdc55-null cells growing at low temperature exhibit a failure of cytokinesis and produce abnormally elongated buds, butcdc55-null cells producing the cyclin-dependent kinase Cdc28-Y19F, which is unable to be inhibited by Y19 phosphorylation, show a loss of the abnormal morphology. Furthermore,cdc55-null cells exhibit a hyperphosphorylation of Y19. For these reasons, we have examined in wild-type and cdc55-null cells the levels and activities of the kinase (Swe1p) and phosphatase (Mih1p) that normally regulate the extent of Cdc28 Y19 phosphorylation. We find that Mih1p levels are comparable in the two strains, and an estimate of the in vivo and in vitro phosphatase activity of this enzyme in the two cell types indicates no marked differences. By contrast, while Swe1p levels are similar in unsynchronized and S-phase-arrested wild-type and cdc55-null cells, Swe1 kinase is found at elevated levels in mitosis-arrestedcdc55-null cells. This excess Swe1p incdc55-null cells is the result of ectopic stabilization of this protein during G2 and M, thereby accounting for the accumulation of Swe1p in mitosis-arrested cells. We also present evidence indicating that, in cdc55-null cells, misregulated PP2A phosphatase activity is the cause of both the ectopic stabilization of Swe1p and the production of the morphologically abnormal phenotype.

scholarly journals The Zds proteins control entry into mitosis and target protein phosphatase 2A to the Cdc25 phosphatase

2011 ◽  
Vol 22 (1) ◽  
pp. 20-32 ◽  
Author(s):  
Sidonie Wicky ◽  
Hendri Tjandra ◽  
David Schieltz ◽  
John Yates ◽  
Douglas R. Kellogg
Keyword(s):  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Regulatory Subunit ◽  
Cyclin Dependent Kinase ◽  
Cdc25 Phosphatase ◽  
Phosphatase 2A ◽  
Wee1 Kinase ◽  
Cycle Dependent ◽  
Related Proteins ◽  
Stoichiometric Complex

The Wee1 kinase restrains entry into mitosis by phosphorylating and inhibiting cyclin-dependent kinase 1 (Cdk1). The Cdc25 phosphatase promotes entry into mitosis by removing Cdk1 inhibitory phosphorylation. Experiments in diverse systems have established that Wee1 and Cdc25 are regulated by protein phosphatase 2A (PP2A), but a full understanding of the function and regulation of PP2A in entry into mitosis has remained elusive. In budding yeast, entry into mitosis is controlled by a specific form of PP2A that is associated with the Cdc55 regulatory subunit (PP2ACdc55). We show here that related proteins called Zds1 and Zds2 form a tight stoichiometric complex with PP2ACdc55and target its activity to Cdc25 but not to Wee1. Conditional inactivation of the Zds proteins revealed that their function is required primarily at entry into mitosis. In addition, Zds1 undergoes cell cycle–dependent changes in phosphorylation. Together, these observations define a role for the Zds proteins in controlling specific functions of PP2ACdc55and suggest that upstream signals that regulate PP2ACdc55may play an important role in controlling entry into mitosis.

Su1989 Inhibition of Protein Phosphatase 2A (PP2A) With LB-100 Enhances the Therapeutic Efficacy of Chemotherapy in Gastric Cancer Cells

2015 ◽  
Vol 148 (4) ◽  
pp. S-569
Author(s):  
Chi Chun Wong ◽  
Liuyang Zhao ◽  
Yun Qian ◽  
Joseph J.Y. Sung ◽  
Jun Yu
Keyword(s):  
Gastric Cancer ◽  
Cancer Cells ◽  
Protein Phosphatase ◽  
Therapeutic Efficacy ◽  
Protein Phosphatase 2A ◽  
Gastric Cancer Cells ◽  
Phosphatase 2A

scholarly journals Regulation of the Cell Cycle by Protein Phosphatase 2A in Saccharomyces cerevisiae

2006 ◽  
Vol 70 (2) ◽  
pp. 440-449 ◽  
Author(s):  
Yu Jiang
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Protein Phosphatase ◽  
Cell Cycle Progression ◽  
Protein Phosphatase 2A ◽  
Cyclin Dependent Kinase ◽  
Cycle Progression ◽  
Phosphatase 2A ◽  
Direct Target ◽  
Cycle Regulation

SUMMARY Protein phosphatase 2A (PP2A) has long been implicated in cell cycle regulation in many different organisms. In the yeast Saccharomyces cerevisiae, PP2A controls cell cycle progression mainly through modulation of cyclin-dependent kinase (CDK) at the G2/M transition. However, CDK does not appear to be a direct target of PP2A. PP2A affects CDK activity through its roles in checkpoint controls. Inactivation of PP2A downregulates CDK by activating the morphogenesis checkpoint and, consequently, delays mitotic entry. Defects in PP2A also compromise the spindle checkpoint and predispose the cell to an error-prone mitotic exit. In addition, PP2A is involved in controlling the G1/S transition and cytokinesis. These findings suggest that PP2A functions in many stages of the cell cycle and its effect on cell cycle progression is pleiotropic.

scholarly journals Protein phosphatase 2A (B55α) prevents premature activation of forkhead transcription factor FoxM1 by antagonizing cyclin A/cyclin-dependent kinase-mediated phosphorylation.

2011 ◽  
Vol 286 (45) ◽  
pp. 39674.2-39674
Author(s):  
Mónica Alvarez-Fernández ◽  
Vincentius A. Halim ◽  
Melinda Aprelia ◽  
Jamila Laoukili ◽  
Shabaz Mohammed ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Cyclin A ◽  
Cyclin Dependent Kinase ◽  
Forkhead Transcription Factor ◽  
Phosphatase 2A

scholarly journals Protein Phosphatase 2A (B55α) Prevents Premature Activation of Forkhead Transcription Factor FoxM1 by Antagonizing Cyclin A/Cyclin-dependent Kinase-mediated Phosphorylation

2011 ◽  
Vol 286 (38) ◽  
pp. 33029-33036 ◽  
Author(s):  
Mónica Alvarez-Fernández ◽  
Vincentius A. Halim ◽  
Melinda Aprelia ◽  
Shabaz Mohammed ◽  
René H. Medema
Keyword(s):  
Transcription Factor ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Cyclin A ◽  
Cyclin Dependent Kinase ◽  
Forkhead Transcription Factor ◽  
Phosphatase 2A
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