Regulation of the AMPK-related protein kinases by ubiquitination.

@article{Thomson2008RegulationOT,
  title={Regulation of the AMPK-related protein kinases by ubiquitination.},
  author={David M. P. Thomson and Marc D. H. Hansen and William Winder},
  journal={The Biochemical journal},
  year={2008},
  volume={411 2},
  pages={e9-10}
}
How can a constitutively active 'master' kinase with numerous downstream targets preferentially phosphorylate one or more of these without influencing all simultaneously? How might such a system be switched off? The characterization of the role of deubiquitination in regulating the phosphorylation and activation of AMPK (AMP-activated protein kinase)-related kinases by LKB1 suggests a novel and interesting mechanism for conferring signal transduction specificity and control at the kinase… CONTINUE READING

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