Serine/Threonine Phosphatases: Mechanism through Structure

@article{Shi2009SerineThreoninePM,
  title={Serine/Threonine Phosphatases: Mechanism through Structure},
  author={Yigong Shi},
  journal={Cell},
  year={2009},
  volume={139},
  pages={468-484}
}
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… CONTINUE READING
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