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Science 28 August 1992: Vol. 257. no. 5074, pp. 1261 - 1264 DOI: 10.1126/science.1325671
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Articles
Science, Vol 257, Issue 5074, 1261-1264
Copyright © 1992 by American Association for the Advancement of Science
Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
J Chen,
BL Martin,
and
DL Brautigan
Division of Biology and Medicine, Brown University, Providence, RI 02912.
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 Tyr307. Phosphorylation was catalyzed by p60v-src, p56lck, 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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- Activation of Mitogen-activated Protein Kinase Cascade Regulates Pituitary Tumor-transforming Gene Transactivation Function.
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- Carboxymethylation of the PP2A Catalytic Subunit in Saccharomyces cerevisiae Is Required for Efficient Interaction with the B-type Subunits Cdc55p and Rts1p.
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