Stimulus-dependent myristoylation of a major substrate for protein kinase C

Bacterial lipopolysaccharide (LPS), the major surface component of gram-negative bacteria, exerts a profound effect on the immune system by enhancing the release of proteins and arachidonic acid metabolites from macrophages (for review see ref. 1). The molecular mechanism(s) by which LPS induces the...

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Bibliographic Details
Published in:Nature (London) 1988-03, Vol.332 (6162), p.362-364
Main Authors: Aderem, Alan A, Albert, Katherine A, Keum, Matthew M, Wang, James K. T, Greengard, Paul, Cohn, Zanvil A
Format: Article
Language:English
Subjects:
Animals
Bacteria
Biological and medical sciences
Cell membranes. Ionic channels. Membrane pores
Cell structures and functions
Fundamental and applied biological sciences. Psychology
Immune system
Lipopolysaccharides - pharmacology
Macrophage Activation - drug effects
Macrophages - metabolism
Metabolites
Mice
Molecular and cellular biology
Myristic Acid
Myristic Acids - metabolism
Phosphorylation
Protein Kinase C - metabolism
Protein Processing, Post-Translational
Proteins
Proteins - metabolism
Substrates
Tetradecanoylphorbol Acetate - pharmacology
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Summary:Bacterial lipopolysaccharide (LPS), the major surface component of gram-negative bacteria, exerts a profound effect on the immune system by enhancing the release of proteins and arachidonic acid metabolites from macrophages (for review see ref. 1). The molecular mechanism(s) by which LPS induces these various secretory responses is unknown. We previously reported that LPS promotes the myristoylation of several macrophage proteins including one with a relative molecular mass (Mr) of 68K2. We have now found that by several criteria the 68K myristoylated protein is similar or identical to the 80/87K protein, a major specific substrate for protein kinase C (PKC) found in brain and fibroblasts (for review see refs 7,8). We have also found that the myristoylated PKC substrate is quantitatively associated with the membrane fraction. Myristoylation of the PKC substrate may target it to the membrane and constitute a transduction pathway for stimulus-response coupling.
ISSN:0028-0836
1476-4687
DOI:10.1038/332362a0