Stoichiometry of the human glycine receptor revealed by direct subunit counting.

Publication Type:

Journal Article

Authors:

Durisic, Nela; Antoine G Godin; Wever, Claudia M; Heyes, Colin D; Lakadamyali, Melike; Dent, Joseph A

Source:

J Neurosci, Volume 32, Issue 37, p.12915-20 (2012)

Keywords:

Animals, Cells, Cultured, Female, Humans, Oocytes, Protein Subunits, Receptors, Glycine, Xenopus laevis

Abstract:

<p>The subunit stoichiometry of heteromeric glycine-gated channels determines fundamental properties of these key inhibitory neurotransmitter receptors; however, the ratio of α1- to β-subunits per receptor remains controversial. We used single-molecule imaging and stepwise photobleaching in Xenopus oocytes to directly determine the subunit stoichiometry of a glycine receptor to be 3α1:2β. This approach allowed us to determine the receptor stoichiometry in mixed populations consisting of both heteromeric and homomeric channels, additionally revealing the quantitative proportions for the two populations.</p>