Serine/Threonine Phosphatases: Mechanism through Structure | Zendy

Yigong Shi | Zendy

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Serine/Threonine Phosphatases: Mechanism through Structure

Author(s) -

Yigong Shi

Publication year - 2009

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2009.10.006

Subject(s) - serine , biology , dephosphorylation , protein phosphatase 2 , phosphorylation , phosphatase , threonine , biochemistry , kinase , phosphoprotein , protein phosphorylation , protein serine threonine kinases , microbiology and biotechnology , protein kinase a

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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