Miller, Stephen G. and Kennedy, Mary B. (1986) Regulation of Brain Type II Ca^(2+)/Calmodulin-Dependent Protein Kinase by Autophosphorylation: A Ca^(2+)-Triggered Molecular Switch. Cell, 44 (6). pp. 861-870. ISSN 0092-8674. http://resolver.caltech.edu/CaltechAUTHORS:20120424-154243496
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Calcium/calmodulin-stimulated autophosphorylation of a prominent brain calmodulin-dependent protein kinase (Type II CaM kinase) produces dramatic changes in its enzymatic activity. These changes suggest a mechanism by which the kinase could act as a calcium-triggered molecular switch. Incorporation of 3-12 of a possible total of 30 phosphate groups per holoenzyme causes kinase activity toward exogenous substrates as well as autophosphorylation itself to become independent of calcium. Thus, kinase activity could be prolonged beyond the duration of an initial activating calcium signal. The calcium-independent autophosphorylation could further prolong the active state by opposing dephosphorylation by cellular phosphatases.
|Additional Information:||© 1986 Elsevier. All rights reserved. Received October 23, 1985; revised December 19, 1985. This investigation was supported in part by the National Institutes of Health Grants NS 17660, IT32 GM07616, and by the Pew Foundation. We thank John Lisman for many useful discussions, Sean Molloy, Bruce Patton, and Venise Radice for help with some of the experiments, and Caren Oto, Lynn Finger, and Candace Hockenedel for help with preparation of the manuscript. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” In accordance with 18 USC. Section 1734 solely to indicate this fact.|
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|Deposited By:||Melanie Stefan|
|Deposited On:||26 Apr 2012 14:38|
|Last Modified:||23 Aug 2016 10:11|
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