Inhibition of protein kinase C- and casein kinase II-mediated phosphorylation of GAP-43 by S100β

Li Hsien Lin, Linda J. Van Eldik, Neil Osheroff, Jeanette J. Norden

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38 Scopus citations


The effect of the glial-derived protein, S100β, on the in vitro phosphorylation of the growth-associated protein GAP-43 was investigated. S100β inhibited in a dose dependent manner the phosphorylation of GAP-43 by protein kinase C (PKC) or by casein kinase II (CKII). S100β appeared to slow down the rate and the degree to which GAP-43 can be phosphorylated by either kinase. The specificity of the inhibition was demonstrated by the observation that the phosphorylation of two other CKII substrates, casein and a selective peptide substrate, was not inhibited by S100β. The marked inhibitory effect of S100β required the presence of calcium in the phosphorylation reactions. In addition, S100β inhibition of GAP-43 phosphorylation was seen with GAP-43 purified under a variety of conditions that alter acylation, suggesting that the acylation state of GAP-43 does not affect the ability of S100β to modulate CKII- or PKC-mediated phosphoryation of GAP-43.

Original languageEnglish
Pages (from-to)297-304
Number of pages8
JournalMolecular Brain Research
Issue number3-4
StatePublished - Sep 1994

Bibliographical note

Funding Information:
These studies were supported in parts by National Institutes of Health Grants AGll138 (to L.V.E.), DK43325 (to N.O.), and NS25150 (to J.J.N.).


  • Acylation
  • Calcium
  • Casein kinase II
  • GAP-43
  • Neuromodulin
  • Phosphorylation
  • Protein kinase C
  • S-100β

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience


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