Serine/threonine phosphatases: mechanism through structure - PubMed (original) (raw)
Review
. 2009 Oct 30;139(3):468-84.
doi: 10.1016/j.cell.2009.10.006.
Affiliations
- PMID: 19879837
- DOI: 10.1016/j.cell.2009.10.006
Free article
Review
Serine/threonine phosphatases: mechanism through structure
Yigong Shi. Cell. 2009.
Free article
Abstract
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.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources