Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-12504
Proc Natl Acad Sci U S A 1999 Aug 17;9617:9891-6. doi: 10.1073/pnas.96.17.9891.
Show Gene links Show Anatomy links

theta, a novel gamma-aminobutyric acid type A receptor subunit.

Bonnert TP , McKernan RM , Farrar S , le Bourdellès B , Heavens RP , Smith DW , Hewson L , Rigby MR , Sirinathsinghji DJ , Brown N , Wafford KA , Whiting PJ .


???displayArticle.abstract???
gamma-Aminobutyric acid type A (GABA-A) receptors are a major mediator of inhibitory neurotransmission in the mammalian central nervous system, and the site of action of a number of clinically important drugs. These receptors exist as a family of subtypes with distinct temporal and spatial patterns of expression and distinct properties that presumably underlie a precise role for each subtype. The newest member of this gene family is the theta subunit. The deduced polypeptide sequence is 627 amino acids long and has highest sequence identity (50.5%) with the beta1 subunit. Within the rat striatum, this subunit coassembles with alpha2, beta1, and gamma1, suggesting that gamma-aminobutyric acid type A receptors consisting of arrangements other than alpha beta + gamma, delta, or epsilon do exist. Expression of alpha2beta1gamma1theta in transfected mammalian cells leads to the formation of receptors with a 4-fold decrease in the affinity for gamma-aminobutyric acid compared with alpha2beta1gamma1. This subunit has a unique distribution, with studies so far suggesting significant expression within monoaminergic neurons of both human and monkey brain.

???displayArticle.pubmedLink??? 10449790
???displayArticle.pmcLink??? PMC22306
???displayArticle.link??? Proc Natl Acad Sci U S A



References [+] :
Backus, Stoichiometry of a recombinant GABAA receptor deduced from mutation-induced rectification. 1993, Pubmed