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Volume 270, Number 12, Issue of March 24, 1995 pp. 6741-6750
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Calmodulin Stabilizes an Amphiphilic -Helix within RC3/Neurogranin and GAP-43/Neuromodulin Only When Ca2+ Is Absent (*)

(Received for publication, November 4, 1994; and in revised form, January 16, 1995)

Dan D. Gerendasy ,  Steven R. Herron ,  Patricia A. Jennings (1),  J. Gregor Sutcliffe (§)

From the Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037 Department of Chemistry and Biochemistry, The University of California, San Diego, La Jolla, California 92093-0301

ABSTRACT

Two neuronal protein kinase C substrates, RC3/neurogranin and GAP-43/neuromodulin, preferentially bind to calmodulin (CaM) when Ca is absent. We examine RC3bulletCaM and GAP-43bulletCaM interactions by circular dichroism spectroscopy using purified, recombinant RC3 and GAP-43, sequence variants of RC3 displaying qualitative and quantitative differences in CaM binding affinities, and overlapping peptides that cumulatively span the entire amino acid sequence of RC3. We conclude that CaM stabilizes a basic, amphiphilic alpha-helix within RC3 and GAP-43 under physiological salt concentrations only when Ca is absent. This provides structural confirmation for two binding modes and suggests that CaM regulates the biological activities of RC3 and GAP-43 through an allosteric, Ca-sensitive mechanism that can be uncoupled by protein kinase C-mediated phosphorylation. More generally, our observations imply an alternative allosteric regulatory role for the Ca-free form of CaM.

FOOTNOTES

*
This work was funded in part by National Institutes of Health Grants NS22111 and NS22347. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked ``advertisement'' in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§
To whom correspondence should be addressed: Dept. of Molecular Biology, The Scripps Research Institute, 10666 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 619-554-8064; Fax: 619-554-6612.

(^1)
The abbreviations used are: CaM, calmodulin; PKC, protein kinase C; 9AC, 9-anthroylcholine; MOPS, 4-morpholinepropanesulfonic acid; TFE, trifluoroethanol.

(^2)
J. B. Watson, unpublished results.

ACKNOWLEDGEMENTS

We gratefully acknowledge Dr. Peter Wright and Dr. Reza Ghadiri for the use their circular dichroism spectrophotometers, Dr. Michael Buchmeier for peptide synthesis and purification, Kerry Guinn and the Scripps Research Institute Protein Service for quantitative amino acid analysis of peptides and purified proteins, Dr. Gary Siuzdak and the mass spectrometry laboratory for analysis of peptides and purified proteins by fast ion bombardment, Dr. Michael Pique and the Molecular Graphics Laboratory for the creation of Fig. 5E and Fig. 6.

©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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