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Casein kinase 2 interacts with human mitogen- and stress-activated protein kinase MSK1 and phosphorylates it at

Yan Shi1, Guanghui Han, Huiling Wu

  • 1State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, 220 Handan Rd, Shanghai 200433, China.

BMB Reports
|January 5, 2010
PubMed

Insights

Mitogen- and stress-activated protein kinase (MSK1) interacts with Casein Kinase 2 (CK2). CK2 phosphorylates MSK1 at multiple C-terminal sites, revealing a new regulatory mechanism for this important kinase.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Mitogen- and stress-activated protein kinase (MSK1) regulates transcription downstream of ERK1/2 and p38 signaling pathways.
  • MSK1 activation involves phosphorylation by ERK1/2 and p38alpha kinases.

Purpose of the Study:

  • To identify novel binding and regulatory partners of MSK1.
  • To investigate the interaction between MSK1 and Casein Kinase 2 (CK2).

Main Methods:

  • Yeast two-hybrid system to detect protein-protein interactions.
  • In vitro and in vivo assays to confirm MSK1-CK2 interactions.
  • Site-directed mutagenesis and mass spectrometry to identify phosphorylation sites.

Main Results:

  • Casein Kinase 2 (CK2) was identified as a binding partner for MSK1.
  • MSK1 interacts with both catalytic (CK2alpha) and regulatory (CK2beta) subunits of CK2.
  • CK2alpha binds to the C-terminal kinase domain of MSK1.
  • CK2 phosphorylates MSK1 at five C-terminal sites (Ser757, Ser758, Ser759, Ser760, Thr793), with four sites being previously unknown.

Conclusions:

  • CK2 is a novel regulatory partner of MSK1.
  • CK2-mediated phosphorylation of MSK1 represents a new layer of regulation for this kinase.
  • These findings expand our understanding of MSK1 signaling pathways.

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