Seven-transmembrane domain receptors

Foord, S. M., and Marshall, F. H. (1999). RAMPS Accessory proteins for seven transmembrane domain receptors. Trends Pharmacol. Sci. 20 184-187. 

FIGURE 18-10 Serpentine (seven-transmembrane-domain) receptors for peptides have binding for their peptide ligands within the membrane... 

Cao, J., Panetta, R., Yue, S., Steyaert, A., Young-BelKdo, M. and Ahmad, S. (2003) A naive Bayes model to predict coupling between seven transmembrane domain receptors and G-proteins. Bioinformatics 19, 234-240. 

Greco NJ, Tandon NN, Jones GD, Komhauser R, Jackson B, Yamamoto N, Tanoue K, Jamiescm GA. Contributions of glycoprotein Ib and the seven transmembrane domain receptor to increases in platdd cytoplasmic [Ca2+] induced by alpha- thrombin. Biochemistry 1996 35 906-14. 

Thrombin will be used as an example of an activator of a seven transmembrane domain receptor. Uptm activation of the receptor, the Gi irotein splits into G and Gp, which both can activate PLCp (Exton, 1994 Brass et al, 1997). Q leads to phosphoinositide hydrolysis and formation of DAG and IP, which activates PKC and en ty C -stores in the endoplasmatic reticulum, respectively. The rise in [Ca causes tyrosine phosfdioi aticHi of the related acbesion focal tyrosine kinase (RAITK.) by an unidentified tyrosine kinase (TK) (Raja et al, 1997). RAFTK can also be tyrosine phosphoiylated by an unknown tyiosiiie kinase (TK.) and activated when PKC is stimulated by phoibol esters... 

Prostanoids act both in an autocrine fashion on the parent cell and in a paracrine fashion on neighboring cells [1,11]. Typically, the role of a prostanoid is to coordinate the responses of the parent cells and neighboring cells to the biosynthetic stimulus — a circulating hormone. The actions of prostanoids are mediated largely by G-protein-linked prostanoid receptors of the seven-transmembrane domain receptor superfamily [11]. 

Loetscher, M., Geiser, T., O Reilly, T., Zwahlen, R., Baggiolini, M., and Moser, B. (1993) Cloning of a human seven transmembrane domain receptor, LESTR, that is highly expressed in leukocytes. J. Biol. Chem. 269, 232-221. 

CBj and CB receptors are members of the superfamily of the seven transmembrane domain receptors that transduce intracellular signals via heterotrimeric GTP-binding proteins. The CB receptor exhibits low amino acid sequence homology with the CBj receptor (44%). Within the transmembrane regions the sequence identity increases to 68%. The CBj receptor is larger than CB, with an additional 72 amino acid residues in the N-terminal region, 15 additional residues in the third extracellular loop, and 13 in the C-terminal region. 

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