A/Prof Antony Cooper
Senior Research Fellow
Antony Cooper is a cell and molecular biologist / geneticist with strong interests in elucidating how cellular dysfunction results in human diseases, with a specific interest in neurodegenerative disease such as Parkinson’s Disease. His research on neurodegenerative diseases focuses on understanding the basis of Parkinson’s Disease.
Antony completed a PhD at McGill University working on membrane trafficking, and post-doctoral studies at the University of Oregon involving both protein splicing and proteostasis/protein quality control in the endoplasmic reticulum (ER). As an Assistant Professor at the University of Missouri his interests evolved to protein misfolding, ER stress and oxidative stress, factors common to many neurodegenerative diseases. As a tenured Associate Professor in Missouri and since returning to Australia at the Garvan Institute he has focused his research on Parkinson’s disease.
- University of Missouri-Kansas City (2002-2006) - Tenured Associate Professor, Cell Biology & Biophysics
- University of Missouri-Kansas City (1996-2002) - Assistant Professor, Cell Biology and Biophysics
- University of Oregon (1991-1995) - Post-doctoral Fellow
In the NewsGarvan Institute marks 200th anniversary of Parkinson’s disease - Apr 11, 2017
Garvan welcomes leading neurogenomics researchers for International Fellow Symposium 2016 - Oct 19, 2016
Identifying genetic factors in bipolar disorder - Oct 15, 2015
2015 St Vincent's Precinct 3 Minute Thesis Competition Held - Jun 19, 2015
Jackie Lau and Louise Cottle win 2014 Stuart Furler Travel Awards - Nov 06, 2014
Garvan receives $15.5 million in NHMRC funding round - Oct 25, 2013
Garvan Institute receives grant to research role of long non-coding RNAs in Parkinson’s disease - Oct 02, 2013
Garvan scientist attracts Michael J Fox Foundation funding - Aug 06, 2012
How yeast is helping us to understand Parkinson's disease - Feb 27, 2009
1984 - BSc (Hons I in Biochemistry), University of Otago - New Zealand
Murphy KE; Gysbers AM; Abbott SK; Spiro AS; Furuta A; Cooper A; Garner B; Kabuta T; Halliday GM, 'Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson's disease', Movement Disorders, 2015; vol. 30, no. 12, pp. 1639 - 1647.
Guennewig B, Cooper AA. The central role of noncoding RNA in the brain. Int Rev Neurobiol. 2014;116:153-94. Review.
Kong SM, Chan BK, Park JS, Hill KJ, Aitken JB, Cottle L, Farghaian H, Cole AR, Lay PA, Sue CM, Cooper AA. Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes. Hum Mol Genet. 2014; Jun 1;23(11):2816-33.
Protter D, Lang C, Cooper AA. αSynuclein and Mitochondrial Dysfunction: A Pathogenic Partnership in Parkinson's Disease? Parkinsons Dis. 2012
Murphy KE; Gysbers AM; Abbott SK; Tayebi N; Kim WS; Sidransky E; Cooper A; Garner B; Halliday GM, 2014, 'Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease', Brain: a journal of neurology, vol. 137, no. 3, pp. 834 - 848
Murphy KE, Cottle L, Gysbers AM, Cooper AA, Halliday GM. ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies. Acta Neuropathol Commun. 2013; 9(1):11.
Protter D, Lang C, Cooper AA. Alpha-Synuclein and Mitochondrial Dysfunction: A Pathogenic Partnership in Parkinson's Disease? Parkinsons Dis. 2012:829207.
Park JS, Mehta P, Cooper A, Veivers D, Heimbach A, Stiller B, Kubisch C, Fung VS, Krainc D, Mackay-Sim A, Sue CM. Pathogenic effects of novel mutations in the Ptype ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset Parkinsonism. Hum Mutat 2011; 32(8):956-64.
Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Su LJ, Auluck PK, Outeiro TF, Yeger-Lotem E, Kritzer JA, Tardiff DF, Strathearn KE, Liu F, Cao S, Hamamichi S, Hill KJ, Caldwell KA, Bell GW, Fraenkel E, Cooper AA, Caldwell GA, McCaffery JM, Rochet JC, Lindquist S. 2010. Disease Models & Mechanisms 3(3-4):194-208.
Gitler AD, Chesi A, Geddie ML, Strathearn KE, Hamamichi S, Hill KJ, Caldwell KA, Cooper AA, Rochet JC, Lindquist S. Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nature Genetics 2009; 41(3): 308-315.
Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, Bhullar B, Liu K, Xu K, Strathearn KE, Liu F, Cao S, Caldwell KA, Caldwell GA, Marsischky G, Kolodner RD, Labaer J, Rochet JC, Bonini NM, Lindquist S. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science 2006; 313:324-8.
Haynes CM, Titus EA, Cooper AA. Accumulation of a Misfolded Protein Leads to Endoplasmic Reticulum Stress and Programmed Cell Death. Molecular Cell 2004; 15(5):767-76.
Haynes CM, Caldwell S, Cooper AA. An HRD1/DER-independent ER Quality Control mechanism involves Rsp5-dependent ubiquitination and ER-Golgi Transport. J Cell Biology 2002; 158:91-101.
Caldwell S Hill KJ & Cooper AA. Degradation of Endoplasmic Reticulum (ER) Quality Control Substrates Requires Transport between the ER and Golgi. J Biol Chem 2001; 276(26):23296-303.
Hill KJ & Cooper AA. Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system. EMBO J. 2000; 19:550-5611.
Cooper AA & Stevens TH. Vps10p Cycles Between the Late Golgi and the Prevacuolar Compartment in its Function as the Sorting Receptor for Multiple Yeast Vacuolar Hydrolyases. J Cell Biol 1996; 133: 529-541.
Piper RC, Cooper AA, Hong H, and Stevens TH. VPS27 Controls Vacuolar and Endocytic Traffic Through a Prevacuolar Compartment in Saccharomyces cerevisiae. J. Cell. Biol. 1995; 131: 603-618.
Cooper AA, Chen YJ, Lindorfer MA, and Stevens TH. Protein Splicing of the Yeast TFP1 Intervening Protein Sequence: a Model for Self-Excision. EMBO J. 1993; 12: 2575- 2583.