|Louise Larose, Ph.D.
Associate Professor, Department of Medicine
louise.larose [at] mcgill.ca
The Larose lab is not taking applications for undergraduate, graduate or post-graduate studies.
I first obtained a M.Sc. degree in Physiology and Biochemistry from the University of Sherbrooke in 1974. My thesis was in the field of the exocrine pancreas. I then was recruited as research assistant by the Department of Biology at the University of Sherbrooke and studied the mechanisms regulating the exocrine pancreatic function for 12 years. In 1988, I joined the laboratory of Dr. André De Léan to pursue my training in the field of the molecular biology of the atrial natriuretic receptor and obtained a Ph.D. degree from the Department of Pharmacology at University of Montreal in 1992. My interests in molecular mechanisms regulating intracellular signal transduction brought me to join the laboratory of Dr. Tony Pawson at the Samuel Lunenfeld Research Institute in Toronto (Ontario) to work as a postdoctoral fellow on receptor tyrosine kinases signaling (1992-95). In 1995, I was recruited as an Assistant Professor in the Department of Medicine, Division of Endocrinology & Metabolism. I was promoted Associate Professor in 2004 and I was awarded FRSQ Chercheur National in 2007. My research focus is on molecular mechanisms regulating cellular responses in physiological and pathological conditions.
Molecular Mechanisms Regulating Intracellular Signaling, Adaptor Proteins, Unfolded Protein Response, Insulin Resistance, Obesity and Diabetes
Research or Clinical Activities
My research interests are on understanding molecular mechanisms involved in signal transduction regulating critical cellular functions such as embryonic development, proliferation, metabolism and response to stress. The research performed by graduate students, postdocs and a research assistant in my laboratory is directed toward the study of the importance of intracellular adaptor molecules that integrate signal transduction pathways by assembling molecular complexes. Particularly, we developed a special interest for the role of the adaptor proteins Nck in molecular mechanisms regulating the unfolded protein response in normal physiological conditions and human pathogenesis associated with impaired glucose homeostasis and insulin biological actions, and the function of the pancreatic beta cells.
Current specific research interests
1. Role of Nck in the pathogenesis of obesity-induced insulin resistance and diabetes.
2. Role of the adaptor Nck in pancreatic beta cells homeostasis.
3. Mechanisms governing the phosphorylation of the adaptor protein Nck.
Selected Recent Publications
Hui*, L., J. Dusseault* and L. Larose. Nck1 depletion induced activation of the PI3K/Akt pathway by attenuating PTP1B protein expression. Cellular Communication and Signaling. October 19, 2014 Supported by CIHR
Yamani*, L., M., Latreille* and L. Larose. Interaction of Nck1 and PERK phosphorylated at Y561 negatively modulates PERK activity and PERK regulation of pancreatic β cell proinsulin content. Molecular Biology of the Cell, 25:702-11, 2014 Epub Dec 26, 2013. Supported by CDA and CIHR. Received 2014 Best Paper Award from McGill Endocrine Division
Latreille, M.*, Abu-Thuraia*, A., Oliva, R.*, Zuo, D.*, and L. Larose. Casein Kinase Iγ2 Impairs Fibroblasts Actin Stress Fibers Formation and Delays Cell Cycle Progression in G1. Int. J. Cell Biol. Focus Issue on Cytoskeleton Proteins. Volume 2012 (2012) ID 684684, 15 pages. Epub 2012 March 7. Supported by CIHR and CDA.
Labelle-Côté*, M., J. Dusseault*, S. Ismaïl*, A. Picard-Cloutier*, P.M. Siegel and L. Larose. Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivo BMC Cancer 11:443-462, 2011 Epub 2011 October 12. Supported by CIHR IF: 3.011
Latreille*, M., M.-K. Laberge*, G. Bourret*, L. Yamani* and L. Larose. Deletion of Nck1 attenuates hepatic ER stress signaling, improves glucose tolerance and insulin signaling in liver of obese mice. Am J Physiol Endocrinol Metab. 300(3):E423-34, 2011. Supported by CDA IF: 4.746