Determinants for Substrate Specificity of Protein Phosphatase 2A

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 subunit...

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Bibliographic Details
Published in:Enzyme Research 2011, Vol.2011 (2011), p.359-366
Main Authors: Slupe, Andrew M., Merrill, Ronald A., Strack, Stefan
Format: Article
Language:English
Subjects:
Cloning
Enzymes
Phosphotransferases
Physiological aspects
Review
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Summary: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.
ISSN:2090-0414
2090-0406
2090-0414
DOI:10.4061/2011/398751