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Related Experiment Videos

Nogo-B is a new physiological substrate for MAPKAP-K2.

Simon Rousseau1, Mark Peggie, David G Campbell

  • 1MRC Protein Phosphorylation Unit, Faculty of Life Sciences, University of Dundee, MSI/WTB Complex, Dow Street, Dundee DD1 5EH, Scotland, UK. s.rousseau@dundee.ac.uk

The Biochemical Journal
|August 13, 2005
PubMed
Summary

Nogo-B protein phosphorylation at Ser107 is induced by stress and inflammation. This process is mediated by MAPKAP-K2 (MAPK-activated protein kinase-2), identifying Nogo-B as its new substrate.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Neuroscience

Background:

  • Nogo is a neurite outgrowth inhibitor with a reticulon homology domain, crucial for endoplasmic reticulum association.
  • The Nogo-B spliceform's function and regulation are not fully understood.

Purpose of the Study:

  • To investigate the post-translational modifications of Nogo-B.
  • To identify the signaling pathways and kinases involved in Nogo-B regulation.

Main Methods:

  • Stimulation of RAW264 macrophages with lipopolysaccharide and HeLa cells with anisomycin.
  • Inhibition studies using SB 203580 and siRNA-mediated knockdown of MAPKAP-K2.
  • In vitro kinase assays using recombinant proteins and analysis of phosphorylation at Ser107.

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Main Results:

  • Nogo-B spliceform undergoes phosphorylation at Ser107 in response to inflammatory and stress stimuli.
  • Phosphorylation is dependent on SAPK2a/p38a signaling and mediated by MAPKAP-K2 and MAPKAP-K3.
  • MAPKAP-K2 directly phosphorylates Nogo-B at Ser107 in vitro.

Conclusions:

  • Nogo-B is a novel physiological substrate of MAPKAP-K2.
  • This finding reveals a new regulatory mechanism for Nogo-B in cellular stress and inflammatory responses.