I obtained my PhD in 2002 and performed postdoctoral work at King’s College London before joining Bruce Kemp’s group at SVI in 2006 to carry out structure/function studies of metabolic kinases. I gained research independence as an ARC Future Fellow in 2014 which was the foundation of the Metabolic Signalling Laboratory. I now hold Honorary positions at The University of Melbourne and Australian Catholic University as Associate Professor.

My group performs research on the roles of critical metabolic kinases and enzymes, how their dysregulation leads to human diseases and how they can be targeted therapeutically. We retain strong research interest in the energy sensor AMPK and its upstream kinase CaMKK2, and more recently have active projects investigating regulation of the mitochondrial fission protein DRP1. These enzymes are important drug targets for metabolic diseases such as type 2 diabetes, cardiovascular disease and liver disease, as well as cancer and neurodegenerative disorders.

The manufacturing arm of my group is also the only global supplier of cation- (P81) and anion- (DE81) exchange papers, essential reagents for gold-standard radiometric assays performed by many research labs and drug screening companies around the world.

Key achievements

2018   The University of Melbourne, Associate Professor; Australian Catholic University, Associate Professor

2014-2017   Australian Research Council Future Fellow


Selected publications

Pinkosky SL, Scott JW, Desjardins EM, Smith BK, Day EA, Ford RJ, Langendorf CG, Ling NXY, Nero TL, Loh K, Galic S, Hoque A, Smiles WJ, Ngoei KRW, Parker MW, Yan Y, Melcher K, Kemp BE, Oakhill JS* & Steinberg GR*. Long-chain fatty acyl-CoA esters regulate metabolism via allosteric control of AMPK beta1 isoforms. *co-senior authors. Nature Metabolism, 2(9):873-881 (2020). DOI: 10.1038/s42255-020-0245-2

Ling NXY, Kaczmarek A, Hoque A, Davie E, Ngoei KRW, Morrison KR, Smiles WJ, Forte GM, Wang T, Lie S, Dite TA, Langendorf CG, Scott JW, Oakhill JS* & Petersen J*. mTORC1 directly inhibits AMPK to promote cell proliferation under nutrient stress. *co-senior authors. Nature Metabolism, 2(1):41-49 (2020). DOI: 10.1038/s42255-019-0157-1

Dite TA, Langendorf CG, Hoque A, Galic S, Rebello RJ, Ovens AJ, Lindqvist LM, Ngoei KRW, Ling NXY, Furic L, Kemp BE, Scott JW & Oakhill JS. AMP-activated protein kinase selectively inhibited by the type II inhibitor SBI-0206965. Journal of Biological Chemistry, 293:8874-8885 (2018). DOI: 10.1074/jbc.RA118.003547

Ngoei KRW, Langendorf CG, Ling NXY, Hoque A, Varghese S, Camerino MA, Walker SR, Bozikis YE, Dite TA, Ovens AJ, Smiles WJ, Jacobs R, Huang H, Parker MW, Scott JW, Rider MH, Foitzik RC, Kemp BE, Baell JB & Oakhill JS. Structural Determinants for Small-Molecule Activation of Skeletal Muscle AMPK α2β2γ1 by the Glucose Importagog SC4. Cell Chemical Biology, 25:728-737 (2018). DOI: 10.1016/j.chembiol.2018.03.008

Dite TA, Ling NXY, Scott JW, Hoque A, Galic S, Parker BL, Ngoei KRW, Langendorf CG, O’Brien MT, Kundu M, Viollet B, Steinberg GR, Sakamoto K, Kemp BE, Oakhill JS. The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs. Nature Communications, 8:571 (2017). DOI: 10.1038/s41467-017-00628-y

Oakhill JS, Steel R, Chen ZP, Scott JW, Ling N, Tam S & Kemp BE. AMPK is a direct adenylate charge-regulated protein kinase. Science, 332:1433-1435 (2011). DOI: 10.1126/science.1200094

ORCID profile: 0000-0002-9475-1440

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The heart of it

October 2023

The heart of it

Congratulations to Associate Professor Jon Oakhill who has been awarded a Heart foundation Vanguard grant to test a potential new drug treatment for a common underlying cause of cardiovascular disease.