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Identifying kinases that target the AMPK drug site

Identifying kinases that target the AMPK drug site

PhD/Honours project

We recently demonstrated that, contrary to well-established models, the master metabolic regulator AMP-activated protein kinase (AMPK) can be activated by drugs even when it is not phoshorylated on Thr172. We determined that drug sensitivity was dependent on phosphorylation of Ser108 in the β-CBM. We now know that Ser108 is a substrate for a small group of kinases from a diverse range of cellular processes including the emerging field of autophagy. Projects are available aimed at characterizing these candidate kinases and evaluating their physiological significance. Training will be provided in a wide range of techniques including protein biochemistry, protein crystallography, mass spectrometry, cell culture, metabolic profiling of genetic mouse models.

Supervised by:

  • Dr Jonathan Oakhill
  • Prof Bruce E. Kemp
  • Dr Christopher Langendorf
  • Disease Focus:

  • Type 2 diabetes
  • Research Unit:

  • Metabolic signalling