PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

FEBS Lett. 1996 Jan 15;378(3):281-5. doi: 10.1016/0014-5793(95)01454-3.

Abstract

The 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) is a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified 'PKC' sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Line
  • Cell-Free System
  • Electrophoresis, Polyacrylamide Gel
  • Glutathione Transferase / genetics
  • Haplorhini
  • Intracellular Signaling Peptides and Proteins*
  • Kidney / cytology
  • Membrane Proteins*
  • Molecular Sequence Data
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Phosphopeptides / chemistry
  • Phosphopeptides / metabolism
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Sequence Analysis
  • Signal Transduction

Substances

  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Peptide Fragments
  • Phosphopeptides
  • Proteins
  • Recombinant Fusion Proteins
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Glutathione Transferase
  • protein kinase N
  • Protein Kinase C