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Enzyme Research
Volume 2011, Article ID 398751, 8 pages
Review Article

Determinants for Substrate Specificity of Protein Phosphatase 2A

Department of Pharmacology, University of Iowa, 2-432 BSB, Iowa City, IA 52242, USA

Received 4 March 2011; Accepted 28 April 2011

Academic Editor: Hemant Paudel

Copyright © 2011 Andrew M. Slupe et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.