Journal
CHEMISTRY & BIOLOGY
Volume 15, Issue 2, Pages 167-174Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2008.01.005
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Funding
- NIGMS NIH HHS [GM57550, R01 GM057550] Funding Source: Medline
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The activity of protein phosphatase 1 (PP1), a serine-threonine phosphatase that participates ubiquitously in cellular signaling, is controlled by a wide variety of regulatory proteins that interact with PP1 at an allosteric regulatory site that recognizes a loose consensus sequence (usually designated as RVXF) found in all such regulatory proteins. Peptides containing the regulatory consensus sequence have been found to recapitulate the binding and PP1 activity modulation of the regulatory proteins, suggesting that it might be possible to design small-molecule surrogates that activate PP1 rather than inhibiting it. This prospect constitutes a largely unexplored way of controlling signaling pathways that could be functionally complementary to the much more extensively explored stratagem of kinase inhibition. Based on these principles, we have designed a microcystin analog that activates PP1.
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