FAM122A, a new endogenous inhibitor of protein phosphatase 2A
Copyright policy )FAM122A, a new endogenous inhibitor of protein phosphatase 2A
The regulation of the ubiquitously expressed protein phosphatase 2A (PP2A) is essential for various cellular functions such as cell proliferation, transformation, and fate determination. In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interacts with PP2A-Aα and B55α rather than B56α subunits, and inhibits the phosphatase activity of PP2A-Aα/B55α/Cα complex. Further, FAM122A potentiates the degradation of catalytic subunit PP2A-Cα with the increased poly-ubiquitination. In agreement, FAM122A silencing inhibits while its overexpression enhances cell growth and colony-forming ability. Collectively, we identify FAM122A as a new endogenous PP2A inhibitor and its physiological and pathophysiological significances warrant to be further investigated.
- Shanghai Jiao Tong University China (People's Republic of)
- Ruijin Hospital, Shanghai Jiaotong University School of Medicine China (People's Republic of)
- Shanghai Institute of Nutrition and Health China (People's Republic of)
- Institute of Health Sciences China (People's Republic of)
- Chinese Academy of Sciences China (People's Republic of)
Intracellular Signaling Peptides and Proteins, Receptor-Like Protein Tyrosine Phosphatases, Class 2, Ubiquitination, Phosphoproteins, Gene Expression Regulation, Neoplastic, Protein Phosphatase 2C, Protein Subunits, HEK293 Cells, A549 Cells, Catalytic Domain, Cell Line, Tumor, Humans, Gene Silencing, Protein Phosphatase 2, Enzyme Inhibitors, Phosphorylation, Protein Processing, Post-Translational, Research Paper, Cell Proliferation, HeLa Cells, Protein Binding
Intracellular Signaling Peptides and Proteins, Receptor-Like Protein Tyrosine Phosphatases, Class 2, Ubiquitination, Phosphoproteins, Gene Expression Regulation, Neoplastic, Protein Phosphatase 2C, Protein Subunits, HEK293 Cells, A549 Cells, Catalytic Domain, Cell Line, Tumor, Humans, Gene Silencing, Protein Phosphatase 2, Enzyme Inhibitors, Phosphorylation, Protein Processing, Post-Translational, Research Paper, Cell Proliferation, HeLa Cells, Protein Binding
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