Literature DB >> 34861123

A comprehensive overview of PPM1A: From structure to disease.

Mao Li1,2, Xingfeng Xu1,2, Yan Su1,2, Xiaoyun Shao2, Yali Zhou3, Jianguo Yan1,2.   

Abstract

PPM1A (magnesium-dependent phosphatase 1 A, also known as PP2Cα) is a member of the Ser/Thr protein phosphatase family. Protein phosphatases catalyze the removal of phosphate groups from proteins via hydrolysis, thus opposing the role of protein kinases. The PP2C family is generally considered a negative regulator in the eukaryotic stress response pathway. PPM1A can bind and dephosphorylate various proteins and is therefore involved in the regulation of a wide range of physiological processes. It plays a crucial role in transcriptional regulation, cell proliferation, and apoptosis and has been suggested to be closely related to the occurrence and development of cancers of the lung, bladder, and breast, amongst others. Moreover, it is closely related to certain autoimmune diseases and neurodegenerative diseases. In this review, we provide an insight into currently available knowledge of PPM1A, including its structure, biological function, involvement in signaling pathways, and association with diseases. Lastly, we discuss whether PPM1A could be targeted for therapy of certain human conditions.

Entities:  

Keywords:  PPM1A; cancer; neurodegenerative diseases; phosphatase; signal pathway

Mesh:

Substances:

Year:  2021        PMID: 34861123      PMCID: PMC8943326          DOI: 10.1177/15353702211061883

Source DB:  PubMed          Journal:  Exp Biol Med (Maywood)        ISSN: 1535-3699


  77 in total

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Journal:  Cell       Date:  1992-06-26       Impact factor: 41.582

2.  Role of protein phosphatase magnesium-dependent 1A and anti-protein phosphatase magnesium-dependent 1A autoantibodies in ankylosing spondylitis.

Authors:  Yong-Gil Kim; Dong Hyun Sohn; Xiaoyan Zhao; Jeremy Sokolove; Tamsin M Lindstrom; Bin Yoo; Chang-Keun Lee; John D Reveille; Joel D Taurog; William H Robinson
Journal:  Arthritis Rheumatol       Date:  2014-10       Impact factor: 10.995

3.  Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases.

Authors:  A Cheng; K E Ross; P Kaldis; M J Solomon
Journal:  Genes Dev       Date:  1999-11-15       Impact factor: 11.361

Review 4.  Negative regulation of RelA phosphorylation: emerging players and their roles in cancer.

Authors:  Xinyuan Lu; Wendell G Yarbrough
Journal:  Cytokine Growth Factor Rev       Date:  2014-10-02       Impact factor: 7.638

5.  Huntingtin phosphorylation on serine 421 is significantly reduced in the striatum and by polyglutamine expansion in vivo.

Authors:  Simon C Warby; Edmond Y Chan; Martina Metzler; Lu Gan; Roshni R Singaraja; Susan F Crocker; Harold A Robertson; Michael R Hayden
Journal:  Hum Mol Genet       Date:  2005-04-20       Impact factor: 6.150

6.  Cell cycle regulation and p53 activation by protein phosphatase 2C alpha.

Authors:  Paula Ofek; Daniella Ben-Meir; Zehavit Kariv-Inbal; Moshe Oren; Sara Lavi
Journal:  J Biol Chem       Date:  2003-01-03       Impact factor: 5.157

7.  A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.

Authors:  Subrata Debnath; Dalibor Kosek; Harichandra D Tagad; Stewart R Durell; Daniel H Appella; Roderico Acevedo; Alexander Grishaev; Fred Dyda; Ettore Appella; Sharlyn J Mazur
Journal:  J Biol Chem       Date:  2018-03-30       Impact factor: 5.157

8.  PPM1A suppresses the proliferation and invasiveness of RCC cells via Smad2/3 signaling inhibition.

Authors:  Yejing Hong; Liangliang Gong; Biying Yu; Yishan Dong
Journal:  J Recept Signal Transduct Res       Date:  2020-09-02       Impact factor: 2.092

9.  Hepatitis C virus NS3 protein enhances hepatocellular carcinoma cell invasion by promoting PPM1A ubiquitination and degradation.

Authors:  Yali Zhou; Yan Zhao; Yaoying Gao; Wenjun Hu; Yan Qu; Ning Lou; Ying Zhu; Xiaoping Zhang; Hongmei Yang
Journal:  J Exp Clin Cancer Res       Date:  2017-03-10

10.  TRIM52 up-regulation in hepatocellular carcinoma cells promotes proliferation, migration and invasion through the ubiquitination of PPM1A.

Authors:  Yi Zhang; Ran Tao; Shan-Shan Wu; Cui-Cui Xu; Jie-Ling Wang; Jie Chen; Yong-Sheng Yu; Zheng-Hao Tang; Xiao-Hua Chen; Guo-Qing Zang
Journal:  J Exp Clin Cancer Res       Date:  2018-06-13
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