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Stéphane A. Laporte, Ph.D.
Interim Director, McGill Division of Endocrinology
Canada Research Chair in Mol. Endocrinology Associate Professor, Dept. of Medicine, and
Dir., Mol. Imaging Pre-Core Facilty, MUHC-RI
McGill University, Polypeptide lab
Strathcona Anatomy & Dentistry Bldg.
Room W315D, 3640 University St.
Montreal, QC H3A 2B2
Tel: 514-398-4487
Fax: 514-398-3923
stephane [dot] laporte [at] mcgill [dot] ca (Email)
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Research:
Hormone and drug action, G protein-coupled receptors, receptor desensitization and trafficking.
My laboratory focuses on studying the molecular and cellular mechanisms regulating G protein-coupled receptors (GPCRs) responses. These receptors are the most commonly targeted class of receptors for drug discovery and therapy, and it is estimated that more than fifty percent of all prescribed drugs today target them. Understanding how different hormones and drugs affect signaling of these receptors still remains a contemporary challenge. Over the past years, our lab has focused on characterizing the functions of beta-arrestin as endocytic and signaling adaptors. We have shown that beta-arrestins recruit structural proteins of the clathrin coat and different kinases to regulate the desensitization, internalization and intracellular trafficking of different GPCRs. Our current work involves delineating the molecular and signaling events regulating the response of GPCRs like the angiotensin II type 1, the beta2-adrenergic and the bradykinin B2 receptors. We use biochemical and molecular imaging approaches such as confocal microscopy to study in real time the dynamics of proteins complexes involved in the internalization, and intracellular trafficking and signaling of these receptors (June, 2007).
Selected Publications:
Fessart D, Simaan M, Hamdan FF, Zimmerman B, Comeau J, Wiseman PW, Bouvier M and Laporte SA. Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex. J Cell Sci. 2007 15; 120(10):1723-32.
Claing A. and SA Laporte. Novel roles for arrestins in GPCR biology and drug discovery. Curr Opin Drug Dis. & Develop. 2005 8(5): 585-9.
Ho J., Cocolakis E., Dumas VM, Posner BI, Laporte SA, Lebrun JJ. The G protein-coupled receptor kinase-2 is a TGFß-inducible antagonist of TGFß signal transduction. EMBO J., 2005 24(18): 3274-58.
Simaan M, Bedard-Goulet S, Fessart D, Gratton JP, Laporte SA. Dissociation of beta-arrestin from internalized bradykinin B2 receptor is necessary for receptor recycling and resensitization. Cell Signal. 2005 17(9): 1074-83.
Fessart D, Simaan M, Laporte SA. c-Src regulates clathrin adapter protein 2 interaction with beta-arrestin and the angiotensin II type 1 receptor during clathrin- mediated internalization. Mol Endocrinol. 2005 19(2): 491-503.
Hasbi A, Devost D, Laporte SA, Zingg HH. Real-time detection of interactions between the human oxytocin receptor and G protein-coupled receptor kinase-2. Mol Endocrinol. 2004 18(5): 1277-86.
Zingg, H.H and Laporte SA. The oxytocin receptor. Trends Endocrinol Metab., 2003 14(5):222-7.