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XB-ART-25401
EMBO J 1990 Dec 01;913:4381-90. doi: 10.1002/j.1460-2075.1990.tb07888.x.
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Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes.

Lechleiter J , Hellmiss R , Duerson K , Ennulat D , David N , Clapham D , Peralta E .


Abstract
Relatively little is understood concerning the mechanisms by which subtypes of receptors, G proteins and effector enzymes interact to transduce specific signals. Through expression of normal, hybrid and deletion mutant receptors in Xenopus oocytes, we determined the G protein coupling characteristics of the functionally distinct m2 and m3 muscarinic acetylcholine receptor (mAChR) subtypes and identified the critical receptor sequences responsible for G protein specificity. Activation of a pertussis toxin insensitive G protein pathway, leading to a rapid and transient release of intracellular Ca2+ characteristic of the m3 receptor, could be specified by the transfer of as few as nine amino acids from the m3 to the m2 receptor. In a reciprocal manner, transfer of no more than 21 residues from the m2 to the m3 receptor was sufficient to specify activation of a pertussis toxin sensitive G protein coupled to a slow and oscillatory Ca2+ release pathway typical of the m2 subtype. Notably, these critical residues occur within the same region of the third cytoplasmic domain of functionally distinct mAChR subtypes.

PubMed ID: 2124972
PMC ID: PMC552228
Article link: EMBO J



References [+] :
Ashkenazi, Functionally distinct G proteins selectively couple different receptors to PI hydrolysis in the same cell. 1989, Pubmed