Biochemical and Biophysical Research Communications
Regular ArticleMutation of an Aspartate at Position 63 in the Human Platelet-Activating Factor Receptor Augments Binding Affinity but Abolishes G-Protein-Coupling and Inositol Phosphate Production1☆,☆☆
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Cited by (24)
Structural features of the G-protein/GPCR interactions
2014, Biochimica et Biophysica Acta - General SubjectsAmino acid residues critical for endoplasmic reticulum export and trafficking of platelet-activating factor receptor
2010, Journal of Biological ChemistryCitation Excerpt :Previously, several groups have demonstrated that the conserved aspartic acid in TM2 is structurally required for G-protein coupling to the receptor in PAFR and other GPCRs (44). For example, Parent et al. (45) reported that substitution of Asp63 to asparagine in PAFR resulted in impairment of the activation of coupled G-proteins without significant alteration of the binding affinity to PAF. In Fig. 5, we obtained supporting results that PAF-elicited Ca2+ mobilization was not observed in D63A expressing cells, although a significant amount of the receptors was trafficked to the cell surface after Y-24180 treatment.
G-protein-independent Activation of Tyk2 by the Platelet-activating Factor Receptor
2001, Journal of Biological ChemistryCitation Excerpt :Co-transfection of Jak2 did not lead to modulation of luciferase activity after PAF stimulation, indicating that this kinase, although activated by PAF, did not play a role in the activation of the minimal PAFR promoter. In order to determine whether G-proteins were necessary for PAF-stimulated transcriptional activation of its receptor, we used mutant receptors (D63N, Y293A, and D289A) that bind the ligand but do not couple to any G-proteins (34-37). Cos-7 cells were transfected with the mutant receptors and p0.16Luc, in the presence or absence of Tyk2 or Jak2.
Selective modulation of wild type receptor functions by mutants of G- protein-coupled receptors
1999, Journal of Biological ChemistryStructural and functional requirements for agonist-induced internalization of the human platelet-activating factor receptor
1997, Journal of Biological Chemistry
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This work was supported by the Medical Research Council of Canada. C.L.G. is supported by a studentship from FCAR.
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The abbreviations used are:G protein, GTP-binding regulatory protein; GPCR, G-protein coupled receptor, GTPγS, guanosine 5′-O-(3-thiotriphosphate); MAP kinase, mitogen-activated protein kinase; PAF, platelet-activating factor; TMH, transmembrane helix; WT, wild-type.
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To whom correspondence should be addressed at Immunology Division, Faculty of Medicine, University of Sherbrooke, 3001 North 12th Avenue, Sherbrooke, Quebec, J1H5N4, Canada Fax: (819) 564-5215.