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Dissociation of phosphorylation and translocation of a myristoylated protein kinase C substrate (MARCKS protein) in C6 glioma and N1E-115 neuroblastoma cells.

Abstract
An 80-kDa protein labeled with [3H]myristic acid in C6 glioma and N1E-115 neuroblastoma cells has been identified as the myristoylated alanine-rich C kinase substrate (MARCKS protein) on the basis of its calmodulin-binding, acidic nature, heat stability, and immunochemical properties. When C6 cells preincubated with [3H]myristate were treated with 200 nM 4 beta-12-O-tetradecanoylphorbol 13-acetate (beta-TPA), labeled MARCKS was rapidly increased in the soluble digitonin fraction (maximal, fivefold at 10 min) with a concomitant decrease in the Triton X-100-soluble membrane fraction. However, phosphorylation of this protein was increased in the presence of beta-TPA to a similar extent in both fractions (maximal, fourfold at 30 min). In contrast, beta-TPA-stimulated phosphorylation of MARCKS in N1E-115 cells was confined to the membrane fraction only and no change in the distribution of the myristoylated protein was noted relative to alpha-TPA controls. These results indicate that although phosphorylation of MARCKS by protein kinase C occurs in both cell lines, it is not directly associated with translocation from membrane to cytosol, which occurs in C6 cells only. The cell-specific translocation of MARCKS appears to correlate with previously demonstrated differential effects of phorbol esters on stimulation of phosphatidylcholine turnover in these two cell lines.
AuthorsD M Byers, F B Palmer, M W Spence, H W Cook
JournalJournal of neurochemistry (J Neurochem) Vol. 60 Issue 4 Pg. 1414-21 (Apr 1993) ISSN: 0022-3042 [Print] England
PMID8455032 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Calmodulin
  • Intracellular Signaling Peptides and Proteins
  • Marcks protein, mouse
  • Marcks protein, rat
  • Membrane Proteins
  • Myristic Acids
  • Proteins
  • Myristic Acid
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate
  • Calcium
Topics
  • Animals
  • Biological Transport
  • Calcium (pharmacology)
  • Calmodulin (metabolism)
  • Cell Membrane (metabolism)
  • Cytosol (metabolism)
  • Drug Stability
  • Glioma (metabolism)
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Membrane Proteins
  • Mice
  • Myristic Acid
  • Myristic Acids (metabolism)
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Neuroblastoma (metabolism)
  • Phosphorylation
  • Protein Kinase C (metabolism)
  • Proteins (metabolism)
  • Rats
  • Tetradecanoylphorbol Acetate (pharmacology)
  • Tumor Cells, Cultured

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