PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163
Copyright policy )PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163
The 80kDa yristolated lanine‐ich ‐inase ubstrate (MARCKS) in 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.
- Johannes Gutenberg University of Mainz Germany
- Institut für Geschichtliche Landeskunde Rheinland-Pfalz e.V. Germany
- Lincoln's Inn United Kingdom
MARCKS, Phosphopeptides, PRK, Recombinant Fusion Proteins, Molecular Sequence Data, Kidney, Cell Line, Protein kinase C, Animals, Amino Acid Sequence, PKC, Phosphorylation, Myristoylated Alanine-Rich C Kinase Substrate, Protein Kinase C, Glutathione Transferase, Binding Sites, Cell-Free System, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Proteins, Haplorhini, Peptide Fragments, Electrophoresis, Polyacrylamide Gel, Sequence Analysis
MARCKS, Phosphopeptides, PRK, Recombinant Fusion Proteins, Molecular Sequence Data, Kidney, Cell Line, Protein kinase C, Animals, Amino Acid Sequence, PKC, Phosphorylation, Myristoylated Alanine-Rich C Kinase Substrate, Protein Kinase C, Glutathione Transferase, Binding Sites, Cell-Free System, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Proteins, Haplorhini, Peptide Fragments, Electrophoresis, Polyacrylamide Gel, Sequence Analysis
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