Form and function in protein dephosphorylation

Article Abstract:

Protein dephosphorylation is a chemical reaction involved in the regulation of physiological processes such as glycogen metabolism, signal transduction, and osmoregulation. There are two classes of enzymes that regulate protein dephosphorylation: protein kinases and protein phosphatases. The latter are further subdivided into two, metallo-protein phosphatases and protein tyrosine phosphatases. An overview of the structure and function of these enzymes is presented.

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Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Article Abstract:

The crystal structures of the protein phosphatase 2A (PP2A) core enzyme bound to two of its inhibitors, the tumor-inducing agents okadaic acid and microcystin-LR, at 2.6 and 2.8 Angstrom resolution respectively are reported. The scaffolding subunit exhibits considerable conformational flexibility, which is proposed to play an important role in PP2A function.

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PPM1A functions as a Smad phosphatase to terminate TGF[beta] signaling

Article Abstract:

PPM1A/PP2C[alpha] is identified as a bona fide Smad phosphate with the help of a functional genomic approach. It is demonstrated that PPM1A/PP2C[alpha], through dephosphorylation of Smad2/3, plays a critical role in terminating TGF[beta] signaling.

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