[HTML][HTML] Serine/threonine phosphatases: mechanism through structure

Y Shi - Cell, 2009 - cell.com
Cell, 2009cell.com
The reversible phosphorylation of proteins is accomplished by opposing activities of kinases
and phosphatases. Relatively few protein serine/threonine phosphatases (PSPs) control the
specific dephosphorylation of thousands of phosphoprotein substrates. Many PSPs,
exemplified by protein phosphatase 1 (PP1) and PP2A, achieve substrate specificity and
regulation through combinatorial interactions between conserved catalytic subunits and a
large number of regulatory subunits. Other PSPs, represented by PP2C and FCP/SCP …
The reversible phosphorylation of proteins is accomplished by opposing activities of kinases and phosphatases. Relatively few protein serine/threonine phosphatases (PSPs) control the specific dephosphorylation of thousands of phosphoprotein substrates. Many PSPs, exemplified by protein phosphatase 1 (PP1) and PP2A, achieve substrate specificity and regulation through combinatorial interactions between conserved catalytic subunits and a large number of regulatory subunits. Other PSPs, represented by PP2C and FCP/SCP, contain both catalytic and regulatory domains within the same polypeptide chain. Here, we discuss biochemical and structural investigations that advance the mechanistic understanding of the three major classes of PSPs, with a focus on PP2A.
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