Determinants for Substrate Specificity of Protein Phosphatase 2A. (2nd July 2011)

• Record Type: Journal Article
• Authors: Slupe, Andrew M.; Merrill, Ronald A.; Strack, Stefan
• Other Names: Paudel Hemant Academic Editor.
• Is Part Of: Enzyme research. Volume 2011(2011)
• Publication Date: 2011-07-02
• Subjects: Enzymes -- Periodicals; 572.7
• DOI: 10.4061/2011/398751
• Languages: English
• ISSNs: 2090-0406

Abstract

Abstract : Protein phosphatase 2A- (PP2A-) catalyzed dephosphorylation of target substrate proteins is widespread and critical for cellular function. PP2A is predominantly found as a heterotrimeric complex of a catalytic subunit (C), a scaffolding subunit (A), and one member of 4 families of regulatory subunits (B). Substrate specificity of the holoenzyme complex is determined by the subcellular locale the complex is confined to, selective incorporation of the B subunit, interactions with endogenous inhibitory proteins, and specific intermolecular interactions between PP2A and target substrates. Here, we discuss recent studies that have advanced our understanding of the molecular determinants for PP2A substrate specificity.