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Calmodulin stabilizes an amphiphilic alpha-helix within rc3/neurogranin and gap-43/neuromodulin only when ca2+ is absent

Academic Article
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Overview

authors

  • Gerendasy, D. D.
  • Herron, S. R.
  • Jennings, P. A.
  • Sutcliffe, J. Gregor

publication date

  • March 1995

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Two neuronal protein kinase C substrates, RC3/neurogranin and GAP-43/neuromodulin, preferentially bind to calmodulin (CaM) when Ca2+ is absent. We examine RC3.CaM and GAP-43.CaM 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 Ca2+ 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(2+)-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(2+)-free form of CaM.

subject areas

  • Allosteric Regulation
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Calcium
  • Calmodulin
  • Calmodulin-Binding Proteins
  • Cattle
  • GAP-43 Protein
  • Membrane Glycoproteins
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Neurogranin
  • Peptide Mapping
  • Protein Kinase C
  • Protein Structure, Secondary
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 7896819
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Additional Document Info

start page

  • 6741

end page

  • 6750

volume

  • 270

issue

  • 12

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