A/Prof Antony Cooper

A/Prof Antony Cooper

Lab Head - Parkinsons Disease and Neurodegeneration

Senior Research Fellow

Conjoint/Adjunct Role(s)

Conjoint Senior Lecturer, School of Biotechnology & Biomolecular Sciences, St Vincent’s Clinical School, UNSW Australia

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.

Previous  Appointments:

  • 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

Research Interests

Parkinson’s Disease; discovering the cause and new approaches to diagnose, treat and cure
Neurogenomics; identifying the genomic and transcriptomic contribution to neurodegenerative diseases
Proteostasis - the integrated cellular pathways that control the biogenesis, folding, trafficking and degradation of proteins
Cellular stresses such as oxidative and nitrosative stress/damage, stress in the endoplasmic reticulum, hypoxia and how they disrupt proteostasis

Education

1990 - PhD in Molecular Biology, McGill University, Montreal - Canada
1984 - BSc (Hons I in Biochemistry), University of Otago - New Zealand

Selected Publications

Murphy KE, Gysbers AM, Abbott SK, Tayebi N, Kim WS, Sidransky E, Cooper AA, Garner B, Halliday GM. Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson’s disease. Brain 2013; (in press)

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. 

A/Prof Antony Cooper