Simon S. Wing



Simon S. Wing, MD, FRCPC

Professor, Endocrinology & Metabolism
Department of Medicine, McGill University
Leader, Metabolic Disorders and Complications Program
Research Institute of the McGill University Health Centre
1001 Decarie Blvd., Room E02.7232, Montreal, QC H4A 3J1

Tel: 514-934-1934 ext. 76184 (Research); 514-934-8224 (Clinic)

simon.wing [at]


Biographical Sketch

MD, CM, McGill University, 1981

Internal Medicine, McGill University, 1984

Endocrinology and Metabolism, McGill University, 1987

Postdoctoral Fellowship, Dept. of Physiology, Harvard Medical School 1987-89

Postdoctoral Fellowship, National Research Council of Canada Biotechnology Research Institute 1990-93

Member, American Society for Clinical Investigation


Ubiquitin, proteasome, muscle wasting, cachexia, metabolism, diabetes, proteolysis, Parkinson’s Disease, neurodegenerative disorders, spermatogenesis

Research or Clinical Activities

Ubiquitin system in skeletal muscle protein degradation

Muscle wasting due to skeletal muscle protein degradation complicates many diseases (e.g. cancer, infection, stroke) as well as normal aging. Our goal is to identify key enzymes in the ubiquitin proteasome system that are responsible for the activation of protein degradation and could be pharmacologically inhibited to prevent or treat muscle wasting. We identified USP19 as a deubiquitinating enzyme that is induced in atrophying skeletal muscle. Our cellular and transgenic knock out studies indicate that this enzyme plays an important role not just in muscle wasting, but has a broader effect on metabolism including physical activity and glucose homeostasis. We are currently exploring mechanisms arid the potential drug targeting of this enzyme.

Ubiquitin system in neurodegenerative disorders

Neurodegenerative disorders such as Parkinson’s and Alzheimer’s Diseases are characterized by the accumulation of protein aggregates in neuronal cells. Accumulation of aggregates is due in part to defective clearance by the proteasome and lysosomal systems. Furthermore, the relentless progression of these disorders appears to be due to the prion like propagation of misfolded proteins from affected cells to adjacent cells by mechanisms that remain poorly defined. We are currently exploring the role of USP19 in mediating both the intracellular clearance of aggregates as well as their propagation.

Selected Recent Publications

Coyne ES, Bedard N, Gong YJ, Faraj M, Tchernof A and Wing SS. The deubiquitinating enzyme USP19 modulates adipogenesis and potentiates high fat diet induced obesity and glucose intolerance in mice. Diabetologia, 2019, 62: 136-146. doi: 10.1007/s00125-018-4754-4

Tessier A-J, Wing SS, Rahme E, Morais JA and Chevalier S. Physical function‐derived cut‐points for the diagnosis of sarcopenia and dynapenia from the Canadian longitudinal study on aging. Journal of Cachexia, Sarcopenia and Muscle, 2019 10:985-999. doi: 10.1002/jcsm.12462.

Coyne ES, Bedard N, Wykes L, Stretch C, Jammoul S, Li S, Zhang K, Sladek RS, Bathe OF, Jagoe RT, Posner BI, Wing SS. Knockout of USP19 Deubiquitinating Enzyme Prevents Muscle Wasting by Modulating Insulin and Glucocorticoid Signaling. Endocrinology 2018, 159:2966-2977.

Bilodeau PA, Coyne ES, and Wing SS. The ubiquitin proteasome system in atrophying muscle – roles and regulation. Amer. J. Physiol. Cell Physiol. 2016, 311:C392-403. (Invited review).

Bédard N, Jammoul S, Moore T, Wykes L, Hallauer PL, Hastings KEM, Stretch C, Baracos V, Chevalier S, Plourde M, Coyne E, Wing SS. Inactivation of the USP19 Deubiquitinating Enzyme Protects Against Muscle Wasting. FASEB J 2015, 29:3889-98. doi: 10.1096/fj.15-270579.

PubMed Publications – S. Wing


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