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

Palmer, R. H., Schonwasser, D. C., Rahman, D., Pappin, D. J., Herget, T., Parker, P. J. (January 1996) PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Febs Letters, 378 (3). pp. 281-5. ISSN 0014-5793

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.

Item Type: Paper
Additional Information: Palmer, R H Schonwasser, D C Rahman, D Pappin, D J Herget, T Parker, P J Netherlands FEBS letters FEBS Lett. 1996 Jan 15;378(3):281-5.
Uncontrolled Keywords: 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 Peptide Fragments/chemistry/metabolism Phosphopeptides/chemistry/metabolism Phosphorylation Protein Kinase C/ metabolism Proteins/isolation & purification/ metabolism Recombinant Fusion Proteins/genetics/isolation & purification/metabolism Sequence Analysis Signal Transduction
Subjects: organs, tissues, organelles, cell types and functions > cell types and functions > cell types > cell line
organs, tissues, organelles, cell types and functions > cell types and functions > cell types > cell line
organs, tissues, organelles, cell types and functions > cell types and functions > cell types > cell line
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > Protein kinase C
organs, tissues, organelles, cell types and functions > tissues types and functions > signal transduction
CSHL Authors:
Communities: CSHL labs > Pappin lab
Depositing User: Kathleen Darby
Date: 15 January 1996
Date Deposited: 13 May 2014 15:20
Last Modified: 13 May 2014 15:20
Related URLs:
URI: https://repository.cshl.edu/id/eprint/30100

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