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p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113

D C Schönwasser1, R H Palmer, T Herget

  • 1Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, London, UK.

FEBS Letters
|October 14, 1996
PubMed

Insights

p42 MAPKinase (MAPK) phosphorylates Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) at Ser-113 in vitro. However, its phosphorylation is not acutely regulated by p42 MAPK in Swiss 3T3 cells.

Area of Science:

  • Cellular signaling pathways
  • Protein phosphorylation
  • Signal transduction

Background:

  • Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is a key substrate in cellular signaling.
  • p42 MAPKinase (MAPK) is a critical enzyme in mitogenic signaling pathways.
  • Regulation of MARCKS phosphorylation by MAPK is not fully understood.

Purpose of the Study:

  • To investigate the phosphorylation of MARCKS at Ser-113 by p42 MAPK.
  • To determine if p42 MAPK acutely regulates MARCKS phosphorylation at Ser-113 in Swiss 3T3 cells.

Main Methods:

  • In vitro kinase assays using p42 MAPK and MARCKS.
  • Analysis of MARCKS phosphorylation in permeabilized Swiss 3T3 cells stimulated with platelet-derived growth factor (PDGF) or activated protein kinase C (PKC).

Main Results:

  • p42 MAPK directly phosphorylates MARCKS at Ser-113 in vitro.
  • Activation of PKC or PDGF stimulation in Swiss 3T3 cells leads to p42 MAPK activation.
  • Despite p42 MAPK activation, only PKC sites on MARCKS are phosphorylated, not Ser-113.

Conclusions:

  • Ser-113 of MARCKS is a substrate for p42 MAPK.
  • Acute regulation of MARCKS Ser-113 phosphorylation by p42 MAPK does not occur in Swiss 3T3 cells under the tested conditions.

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