Phosphorylation of MARCKS, neuromodulin, and neurogranin by protein kinase C exhibits differential responses to diacylglycerols.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Author(s): Mahoney CW;Mahoney CW; Seki K; Huang KP
  • Source:
    Cellular signalling [Cell Signal] 1995 Sep; Vol. 7 (7), pp. 679-85.
  • Publication Type:
    Comparative Study; Journal Article
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Science Ltd Country of Publication: England NLM ID: 8904683 Publication Model: Print Cited Medium: Print ISSN: 0898-6568 (Print) Linking ISSN: 08986568 NLM ISO Abbreviation: Cell Signal Subsets: MEDLINE
    • Publication Information:
      Publication: Oxford : Elsevier Science Ltd
      Original Publication: Oxford ; New York : Pergamon Press, 1988-
    • Subject Terms:
      Intracellular Signaling Peptides and Proteins* ; Membrane Proteins*; Calmodulin-Binding Proteins/*metabolism ; Diglycerides/*pharmacology ; Membrane Glycoproteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Protein Kinase C/*metabolism ; Proteins/*metabolism; Animals ; Brain/drug effects ; Brain/metabolism ; Enzyme Activation/drug effects ; GAP-43 Protein ; Myristoylated Alanine-Rich C Kinase Substrate ; Neurogranin ; Phosphoproteins/metabolism ; Phosphorylation ; Rats
    • Abstract:
      Diacylglycerols (DG) derived from brain phosphatidylinositol (PI) and phosphatidylcholine (PC) and synthetic 1,2-dioleoylglycerol (diC18:1) and 1,2-dioctanoylglycerol (diC8) were tested for their efficacy in stimulating PKC-catalyzed phosphorylation of three physiological substrates in the brain, namely, MARCKS, neuromodulin (Nm), and neurogranin (Ng). The A0.5 of these DGs for PKC were variable dependent on the protein substrates; the values were lowest with MARCKS and highest with Ng. With Ng as a substrate the A0.5 of these DGs for PKC gamma were PI- and PC-DGs < diC18:1 < diC8. Both PI- and PC-DGs, in spite of their differences in unsaturated fatty acids content, were similarly effective in stimulating PKC. Since the phosphorylation of MARCKS, as compared to those of Nm and Ng, has the lowest A0.5 with the various DGs, it seems that among these three PKC substrates MARCKS is most readily phosphorylated by PKCs following DG formation in vivo.
    • Accession Number:
      0 (Calmodulin-Binding Proteins)
      0 (Diglycerides)
      0 (GAP-43 Protein)
      0 (Intracellular Signaling Peptides and Proteins)
      0 (Marcks protein, rat)
      0 (Membrane Glycoproteins)
      0 (Membrane Proteins)
      0 (Nerve Tissue Proteins)
      0 (Nrgn protein, rat)
      0 (Phosphoproteins)
      0 (Proteins)
      125267-21-2 (Myristoylated Alanine-Rich C Kinase Substrate)
      132654-77-4 (Neurogranin)
      EC 2.7.11.13 (Protein Kinase C)
    • Publication Date:
      Date Created: 19950901 Date Completed: 19960124 Latest Revision: 20190920
    • Publication Date:
      20231215
    • Accession Number:
      10.1016/0898-6568(95)00043-o
    • Accession Number:
      8519597