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Calmodulin influences MAPK signaling by binding KSR1.

Swetha Parvathaneni1, Zhigang Li1, David B Sacks1

  • 1Department of Laboratory Medicine, National Institutes of Health, Bethesda, Maryland, USA.

The Journal of Biological Chemistry
|March 26, 2021
PubMed
Summary

Calcium ions regulate the MAPK pathway by affecting the scaffold protein KSR1. This study shows calcium is required for calmodulin to bind KSR1, impacting ERK activation and cell signaling.

Keywords:
calciumcalmodulinkinase suppressor of Ras1 (KSR1)mitogen-activated protein kinase (MAPK)protein–protein interactionsignaling

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Area of Science:

  • Cellular signaling
  • Molecular biology
  • Biochemistry

Background:

  • Mitogen-activated protein kinase (MAPK) pathways control cell fate.
  • Scaffold proteins like KSR1 regulate MAPK activation by growth factors.
  • Calcium's role in MAPK signaling is not fully understood.

Purpose of the Study:

  • To investigate if calcium alters MAPK activity through KSR1.
  • To explore the interaction between KSR1 and calmodulin.

Main Methods:

  • In vitro protein binding assays.
  • Co-immunoprecipitation from mammalian cell lysates.
  • Confocal microscopy.
  • Use of a cell-permeable calmodulin antagonist (CGS9343B).

Main Results:

  • Calmodulin directly binds KSR1 in a calcium-dependent manner.
  • Calcium is essential for calmodulin-KSR1 association in vitro and in cells.
  • Inhibiting calmodulin reduced EGF-induced ERK activation and KSR1 translocation.

Conclusions:

  • Calcium signaling influences the MAPK pathway via the KSR1 scaffold protein.
  • Calmodulin binding to KSR1 is a key calcium-dependent regulatory step.
  • This identifies a novel mechanism linking calcium and MAPK cascades.