PAR1 Thrombin Receptor-G Protein Interactions
نویسندگان
چکیده
منابع مشابه
PAR1 thrombin receptor-G protein interactions. Separation of binding and coupling determinants in the galpha subunit.
Signal transfer between the protease-activated PAR1 thrombin receptor and membrane-associated heterotrimeric G proteins is mediated by protein-protein interactions. We constructed a yeast signaling system that resolves domain-specific functions of binding from coupling in the Galpha subunit. The endogenous yeast Galpha subunit, Gpa1, does not bind to PAR1 and served as a null structural templat...
متن کاملG-protein Coupled Receptor Dimerization
A growing body of evidence suggests that GPCRs exist and function as dimers or higher oligomers. The evidence for GPCR dimerization comes from biochemical, biophysical and functional studies. In addition, researchers have shown the occurrence of heterodimerization between different members of the GPCR family. Two receptors can interact with each other to make a dimer through their extracellular...
متن کاملEngineering thrombin for selective specificity toward protein C and PAR1.
Thrombin elicits functional responses critical to blood homeostasis by interacting with diverse physiological substrates. Ala-scanning mutagenesis of 97 residues covering 53% of the solvent accessible surface area of the enzyme identifies Trp(215) as the single most important determinant of thrombin specificity. Saturation mutagenesis of Trp(215) produces constructs featuring k(cat)/K(m) values...
متن کاملRethinking receptor-G protein-effector interactions.
Hundreds of different receptors regulate the activity of effector proteins with the assistance of heterotrimeric guanine nucleotide-binding proteins (G proteins). The hypothesis that G protein-coupled receptors (R) govern their effectors (E) indirectly via a shuttling mechanism involving the exchange of heterotrimeric G proteins (G[alpha betagamma]) or parts thereof (G[alpha], G[betagamma]) bet...
متن کاملProtease-activated receptor 1 (PAR1) and PAR4 heterodimers are required for PAR1-enhanced cleavage of PAR4 by α-thrombin.
Thrombin is a potent platelet agonist that activates platelets and other cells of the cardiovascular system by cleaving its G-protein-coupled receptors, protease-activated receptor 1 (PAR1), PAR4, or both. We now show that cleaving PAR1 and PAR4 with α-thrombin induces heterodimer formation. PAR1-PAR4 heterodimers were not detected when unstimulated; however, when the cells were stimulated with...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.275.4.2627