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Updated: Mar 31, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
Published on: August 13, 2017
All roads lead to PP2A: exploiting the therapeutic potential of this phosphatase
Jaya Sangodkar1, Caroline C Farrington2, Kimberly McClinch3
1Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York City, NY, USA.
Abstract:
Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase involved in the regulation of many cellular processes. A confirmed tumor suppressor protein, PP2A is genetically altered or functionally inactivated in many cancers highlighting a need for its therapeutic reactivation. In this review we discuss recent literature on PP2A: the elucidation of its structure and the functions of its subunits, and the identification of molecular lesions and post-translational modifications leading to its dysregulation in cancer. A final section will discuss the proteins and small molecules that modulate PP2A and how these might be used to target dysregulated forms of PP2A to treat cancers and other diseases.
Insights
Protein phosphatase 2A (PP2A) is a tumor suppressor crucial for cellular processes. This review explores PP2A
Area of Science:
- Molecular biology
- Biochemistry
- Oncology
Background:
- Protein phosphatase 2A (PP2A) regulates numerous cellular functions.
- PP2A acts as a tumor suppressor, and its inactivation is common in cancers.
- Therapeutic strategies to restore PP2A function are needed for cancer treatment.
Purpose of the Study:
- To review recent literature on Protein phosphatase 2A (PP2A).
- To discuss PP2A structure, subunit functions, and cancer-related dysregulation.
- To explore therapeutic targets modulating PP2A for cancer treatment.
Main Methods:
- Literature review of recent scientific publications.
- Analysis of structural and functional data of PP2A.
- Examination of molecular mechanisms of PP2A dysregulation in cancer.
Main Results:
- Recent studies have elucidated PP2A structure and subunit roles.
- Molecular lesions and post-translational modifications contribute to PP2A dysregulation in cancer.
- Proteins and small molecules modulating PP2A are identified.
Conclusions:
- Understanding PP2A's structure and function is key to its therapeutic reactivation.
- Targeting dysregulated PP2A offers potential treatment strategies for cancers.
- Modulators of PP2A may be useful in treating various diseases.
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