M
Michel Bouvier
Researcher at Université de Montréal
Publications - 412
Citations - 33931
Michel Bouvier is an academic researcher from Université de Montréal. The author has contributed to research in topics: Receptor & G protein-coupled receptor. The author has an hindex of 97, co-authored 396 publications receiving 31267 citations. Previous affiliations of Michel Bouvier include École Polytechnique de Montréal & University of Catania.
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Journal ArticleDOI
Receptor-regulated Interaction of Activator of G-protein Signaling-4 and Gαi
TL;DR: Data suggest that AGS4-Gαi complexes directly couple to a G-protein-coupled receptor and may serve as substrates for agonist-induced G- protein activation.
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Receptor-regulated interaction of activator of g-protein signaling 4 and gialpha
TL;DR: In this paper, the activation of G-protein signaling-4 (AGS4) with Gαi1 was evaluated using bioluminescence resonance energy transfer (BRET).
Journal ArticleDOI
Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex.
Delphine Fessart,May Simaan,Brandon Zimmerman,Jonathan W.D. Comeau,Fadi F. Hamdan,Paul W. Wiseman,Michel Bouvier,Stéphane A. Laporte +7 more
TL;DR: These findings not only unveil β2-adaptin as a new Src target during AT1R internalization, but also support the role of receptor-mediated signaling in the control of clathrin-dependent endocytosis of receptors.
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Spatiotemporal regulation of the GPCR activity of BAI3 by C1qL4 and Stabilin-2 controls myoblast fusion
Noumeira Hamoud,Viviane Tran,Takahiro Aimi,Wataru Kakegawa,Sylvie Lahaie,Sylvie Lahaie,Marie Pier Thibault,Ariane Pelletier,G. William Wong,In San Kim,In San Kim,Artur Kania,Artur Kania,Michisuke Yuzaki,Michel Bouvier,Jean-François Côté,Jean-François Côté +16 more
TL;DR: It is shown that the GPCR activity of BAI3 is spatiotemporally regulated during myoblast fusion, and C1qL4 and Stabilin-2 are identified as negative and positive regulators of its activity.
Journal Article
Distinct receptor domains determine subtype-specific coupling and desensitization phenotypes for human beta1- and beta2-adrenergic receptors.
TL;DR: The results suggest that the carboxyl portion of the beta1 AR and beta2 AR determines their subtype-selective desensitization patterns but not their respective coupling efficacies.