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Science 22 May 1992:
Vol. 256. no. 5060, pp. 1199 - 1202
DOI: 10.1126/science.256.5060.1199
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Articles

Calmodulin Trapping by Calcium-Calmodulin-Dependent Protein Kinase

Tobias Meyer 1, Phyllis I. Hanson 2, Lubert Stryer 1, and Howard Schulman 2

1 Department of Cell Biology, Stanford University School of Medicine, Stanford, CA 94305
2 Department of Pharmacology, Stanford University School of Medicine, Stanford, CA 94305

Multifunctional calcium-calmodulin-dependent protein kinase (CaM kinase) transduces transient elevations in intracellular calcium into changes in the phosphorylation state and activity of target proteins. By fluorescence emission anisotropy, the affinity of CaM kinase for dansylated calmodulin was measured and found to increase 1000 times after autophosphorylation of the threonine at position 286 of the protein. Autophosphorylation markedly slowed the release of bound calcium-calmodulin; the release time increased from less than a second to several hundred seconds. In essence, calmodulin is trapped by autophosphorylation. The shift in affinity does not occur in a site-directed mutant in which threonine at position 286 has been replaced by a non-phosphorylatable amino acid. These experiments demonstrate the existence of a new state in which calmodulin is bound to CaM kinase even though the concentration of calcium is basal. Calmodulin trapping provides for molecular potentiation of calcium transients and may enable detection of their frequency.


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S. I. Singla, A. Hudmon, J. M. Goldberg, J. L. Smith, and H. Schulman (2001)
J. Biol. Chem. 276, 29353-29360
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Cellular Signaling through Multifunctional Ca2+/Calmodulin-dependent Protein Kinase II.
T. R. Soderling, B. Chang, and D. Brickey (2001)
J. Biol. Chem. 276, 3719-3722
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Science. ISSN 0036-8075 (print), 1095-9203 (online)