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Regulation of Protein Serine-Threonine Phosphatase Type-2A by Tyrosine Phosphorylation

Jian Chen, Bruce L. Martin and David L. Brautigan
Science
New Series, Vol. 257, No. 5074 (Aug. 28, 1992), pp. 1261-1264
Stable URL: http://www.jstor.org/stable/2880034
Page Count: 4
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Regulation of Protein Serine-Threonine Phosphatase Type-2A by Tyrosine Phosphorylation
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Abstract

Extracellular signals that promote cell growth activate cascades of protein kinases. The kinases are dephosphorylated and deactivated by a single type-2A protein phosphatase. The catalytic subunit of type-2A protein phosphatase was phosphorylated by tyrosine-specific protein kinases. Phosphorylation was enhanced in the presence of the phosphatase inhibitor okadaic acid, consistent with an autodephosphorylation reaction. More than 90% of the activity of phosphatase 2A was lost when thioadenosine triphosphate was used to produce a thiophosphorylated protein resistant to autodephosphorylation. Phosphorylation in vitro occurred exclusively on Tyr$^{307}$. Phosphorylation was catalyzed by p60$^{v-src}$, p56$^{lck}$, epidermal growth factor receptors, and insulin receptors. Transient deactivation of phosphatase 2A might enhance transmission of cellular signals through kinase cascades within cells.

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