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PP2A holoenzyme assembly:in cauda venenum(the sting is in the tail)

Authors
Journal
Trends in Biochemical Sciences
0968-0004
Publisher
Elsevier
Publication Date
Volume
33
Issue
3
Identifiers
DOI: 10.1016/j.tibs.2007.12.004
Disciplines
  • Biology
  • Chemistry
  • Medicine

Abstract

Protein phosphatase 2A (PP2A), a major phospho-serine/threonine phosphatase, is conserved throughout eukaryotes. It dephosphorylates a plethora of cellular proteins, including kinases and other signaling molecules involved in cell division, gene regulation, protein synthesis and cytoskeleton organization. PP2A enzymes typically exist as heterotrimers comprising catalytic C-, structural A- and regulatory B-type subunits. The B-type subunits function as targeting and substrate-specificity factors; hence, holoenzyme assembly with the appropriate B-type subunit is crucial for PP2A specificity and regulation. Recently, several biochemical and structural determinants have been described that affect PP2A holoenzyme assembly. Moreover, the effects of specific post-translational modifications of the C-terminal tail of the catalytic subunit indicate that a ‘code’ might regulate dynamic exchange of regulatory B-type subunits, thus affecting the specificity of PP2A.

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