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

V Janssens, S Longin, J Goris - Trends in biochemical sciences, 2008 - cell.com
V Janssens, S Longin, J Goris
Trends in biochemical sciences, 2008cell.com
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 …
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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