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Role of the highly conserved Asp‐Arg‐Tyr motif in signal transduction of the CB 2 cannabinoid receptor
Author(s) -
Rhee Man-Hee,
Nevo Igal,
Levy Rivka,
Vogel Zvi
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01094-2
Subject(s) - adenylyl cyclase , cannabinoid receptor type 2 , receptor , signal transduction , cannabinoid , cannabinoid receptor , g protein coupled receptor , chemistry , agonist , intracellular , g protein , transmembrane domain , microbiology and biotechnology , biology , biochemistry
The DRY motif, at the junction of transmembrane helix 3 and intracellular loop 2 of G protein‐coupled receptors, is highly conserved. Mutations were introduced into the CB 2 cannabinoid receptor to study the role of this motif in CB 2 signaling. D mutations (DRY130–132AAA and D130A) markedly reduced binding of cannabinoid agonists, while no significant reduction was observed with R131A or Y132A. Mutating R (R131A) only partially reduced, and mutating Y (Y132A) more efficiently reduced the cannabinoid‐induced inhibition of adenylyl cyclase. Thus, in CB 2 , D130 is involved in agonist binding, whereas Y seems to have a role in receptor downstream signaling.