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- Title
Asymmetric conformational changes in a GPCR dimer controlled by G-proteins.
- Authors
Damian, Marjorie; Martin, Aimée; Mesnier, Danielle; Pin, Jean-Philippe; Banères, Jean-Louis
- Abstract
G-protein-coupled receptors (GPCRs) are key players in cell communication. Although long considered as monomeric, it now appears that these heptahelical proteins can form homo- or heterodimers. Here, we analyzed the conformational changes in each subunit of a receptor dimer resulting from agonist binding to either one or both subunits by measuring the fluorescent properties of a leukotriene B4 receptor dimer with a single 5-hydroxytryptophan-labeled protomer. We show that a receptor dimer with only a single agonist-occupied subunit can trigger G-protein activation. We also show that the two subunits of the receptor dimer in the G-protein-coupled state differ in their conformation, even when both are liganded by the agonist. No such asymmetric conformational changes are observed in the absence of G-protein, indicating that the interaction of the G-protein with the receptor dimer brings specific constraints that prevent a symmetric functioning of this dimer. These data open new options for the differential signaling properties of GPCR dimers.
- Subjects
CELLULAR signal transduction; BIOENERGETICS; SYMMETRY (Biology); PROTEINS; CELL communication; CELLULAR control mechanisms; CELL receptors
- Publication
EMBO Journal, 2006, Vol 25, Issue 24, p5693
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1038/sj.emboj.7601449