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Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence.

Publication ,  Journal Article
Edelman, AM; Mitchelhill, KI; Selbert, MA; Anderson, KA; Hook, SS; Stapleton, D; Goldstein, EG; Means, AR; Kemp, BE
Published in: J Biol Chem
May 3, 1996

We have purified to near homogeneity from rat brain two Ca(2+)-calmodulin-dependent protein kinase I (CaM kinase I) activating kinases, termed here CaM kinase I kinase-alpha and CaM kinase I kinase-beta (CaMKIK alpha and CaMKIK beta, respectively). Both CaMKIK alpha and CaMKIK beta are also capable of activating CaM kinase IV. Activation of CaM kinase I and CaM kinase IV occurs via phosphorylation of an equivalent Thr residue within the "activation loop" region of both kinases, Thr-177 and Thr-196, respectively. The activities of CaMKIK alpha and CaMKIK beta are themselves strongly stimulated by the presence of Ca(2+)-CaM, and both appear to be capable of Ca(2+)-CaM-dependent autophosphorylation. Automated microsequence analysis of the purified enzymes established that CaMKIK alpha and -beta are the products of distinct genes. In addition to rat, homologous nucleic acids corresponding to these CaM kinase kinases are present in humans and the nematode, Caenorhabditis elegans. CaMKIK alpha and CaMKIK beta are thus representatives of a family of enzymes, which may function as key intermediaries in Ca(2+)-CaM-driven signal transduction cascades in a wide variety of eukaryotic organisms.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

May 3, 1996

Volume

271

Issue

18

Start / End Page

10806 / 10810

Location

United States

Related Subject Headings

  • Sequence Homology, Amino Acid
  • Rats, Sprague-Dawley
  • Rats
  • Molecular Sequence Data
  • Isoenzymes
  • Enzyme Activation
  • Chromatography, Liquid
  • Calmodulin
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Calcium
 

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Edelman, A. M., Mitchelhill, K. I., Selbert, M. A., Anderson, K. A., Hook, S. S., Stapleton, D., … Kemp, B. E. (1996). Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence. J Biol Chem, 271(18), 10806–10810. https://doi.org/10.1074/jbc.271.18.10806
Edelman, A. M., K. I. Mitchelhill, M. A. Selbert, K. A. Anderson, S. S. Hook, D. Stapleton, E. G. Goldstein, A. R. Means, and B. E. Kemp. “Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence.J Biol Chem 271, no. 18 (May 3, 1996): 10806–10. https://doi.org/10.1074/jbc.271.18.10806.
Edelman AM, Mitchelhill KI, Selbert MA, Anderson KA, Hook SS, Stapleton D, et al. Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence. J Biol Chem. 1996 May 3;271(18):10806–10.
Edelman, A. M., et al. “Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence.J Biol Chem, vol. 271, no. 18, May 1996, pp. 10806–10. Pubmed, doi:10.1074/jbc.271.18.10806.
Edelman AM, Mitchelhill KI, Selbert MA, Anderson KA, Hook SS, Stapleton D, Goldstein EG, Means AR, Kemp BE. Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence. J Biol Chem. 1996 May 3;271(18):10806–10810.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

May 3, 1996

Volume

271

Issue

18

Start / End Page

10806 / 10810

Location

United States

Related Subject Headings

  • Sequence Homology, Amino Acid
  • Rats, Sprague-Dawley
  • Rats
  • Molecular Sequence Data
  • Isoenzymes
  • Enzyme Activation
  • Chromatography, Liquid
  • Calmodulin
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Calcium