PP2A-B55 Holoenzyme Regulation and Cancer

被引:15
作者
Goguet-Rubio, Perrine [1 ]
Amin, Priya [1 ]
Awal, Sushil [1 ]
Vigneron, Suzanne [1 ]
Charrasse, Sophie [1 ]
Mechali, Francisca [1 ]
Labbe, Jean Claude [1 ]
Lorca, Thierry [1 ]
Castro, Anna [1 ]
机构
[1] Univ Montpellier, Equipe Labellisee Ligue Natl Canc, Ctr Rech Biol Cellulaire Montpellier CRBM, CNRS UMR 5237, 1919 Route Mende, F-34293 Montpellier 5, France
关键词
PP2A-B55; cancer; Greatwall; Arpp19; ENSA; PROTEIN PHOSPHATASE 2A; CATALYTIC SUBUNIT; SACCHAROMYCES-CEREVISIAE; GREATWALL KINASE; T308; PHOSPHORYLATION; CELL-PROLIFERATION; SET ONCOPROTEIN; T-ANTIGEN; INHIBITOR; EXPRESSION;
D O I
10.3390/biom10111586
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein phosphorylation is a post-translational modification essential for the control of the activity of most enzymes in the cell. This protein modification results from a fine-tuned balance between kinases and phosphatases. PP2A is one of the major serine/threonine phosphatases that is involved in the control of a myriad of different signaling cascades. This enzyme, often misregulated in cancer, is considered a tumor suppressor. In this review, we will focus on PP2A-B55, a particular holoenzyme of the family of the PP2A phosphatases whose specific role in cancer development and progression has only recently been highlighted. The discovery of the Greatwall (Gwl)/Arpp19-ENSA cascade, a new pathway specifically controlling PP2A-B55 activity, has been shown to be frequently altered in cancer. Herein, we will review the current knowledge about the mechanisms controlling the formation and the regulation of the activity of this phosphatase and its misregulation in cancer.
引用
收藏
页码:1 / 17
页数:17
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