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Sequences of autophosphorylation sites in neuronal type II CaM kinase that control Ca^(2+)-independent activity.

Miller, Stephen G. and Patton, Bruce L. and Kennedy, Mary B. (1988) Sequences of autophosphorylation sites in neuronal type II CaM kinase that control Ca^(2+)-independent activity. Neuron, 1 (7). pp. 593-604. ISSN 0896-6273. http://resolver.caltech.edu/CaltechAUTHORS:20120424-154239342

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Abstract

After initial activation by Ca^(2+), the catalytic activity of type II Ca^(2+)/calmodulin-dependent protein kinase rapidly becomes partially independent of Ca^(2+). The transition is caused by autophosphorylation of a few subunits in the dodecameric holoenzyme, which is composed of varying proportions of two homologous types of subunits, alpha (50 kd) and beta (58-60 kd). We have identified one site in the alpha subunit (Thr286) and two in the beta subunit (Thr287 and Thr382) that are rapidly autophosphorylated. We show that phosphorylation of alpha-Thr286 and beta-Thr287, which are located immediately adjacent to the calmodulin binding domain, controls Ca^(2+)-independent activity. In contrast, phosphorylation of beta-Thr382 is not required to maintain Ca2+ independence. It is absent in the alpha subunit and is selectively removed from the minor beta' subunit, apparently by alternative splicing. Regulation of the presence of beta-Thr382 in the holoenzyme by both differential gene expression and alternative splicing suggests that it may have an important but highly specialized function.


Item Type:Article
Additional Information:Elsevier Copyright © 1988. Received 13 June 1988. Revised 19 July 1988. Available online 7 September 2004. We thank Dr. Rudi Aebersold for advice during the early stages of this study and Dr. M. McMillan and L. Williams of the University of Southern California Comprehensive Cancer Center Microchemical Facility (Los Angeles, CA), Dr. E. Weber of the Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University (Portland, OR), and Dr. D. Teplow, J. Racs, and H. Wong of the California Institute of Technology Applied Microsequencing Facility !Pasadena, CA) for peptide sequencing and amino acid analysis. We also thank Caroline Bell for help with preparation of the manuscript. This work was supported by NIH grants NST7660 and NS07251. by the McKnight Foundation, and by the Epilepsy Foundation of America.
Funders:
Funding AgencyGrant Number
NIHNST7660
NIHNS07251
McKnight FoundationUNSPECIFIED
Epilepsy Foundation of AmericaUNSPECIFIED
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ID Code:30345
Collection:CaltechAUTHORS
Deposited By: Melanie Stefan
Deposited On:25 Apr 2012 17:24
Last Modified:25 Apr 2012 19:03

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