Referenced in: none

Automatically associated channels: Slo1

Title: Single-channel study of the binding-gating coupling in the slowly desensitizing chimeric alpha7-5HT3A receptor.

Authors: José Antonio Bernal, José Mulet, Mar Castillo, Manuel Criado, Francisco Sala, Salvador Sala

Journal, date & volume: FEBS Lett., 2009 Mar 18 , 583, 1045-51

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/19236866

Abstract
We have studied the role of the highly conserved residue alphaLysine145 in the early steps of activation by acetylcholine of the nicotinic acetylcholine receptor (nAChR). Both macroscopic and single-channel currents were recorded in the slowly desensitizing chimeric mutant receptor alpha7V201-5HT3A/R432Q/R436D/R440A, made of alpha7 nAChRs and serotonin receptors of subtype 3A (ch1), and its corresponding mutant K145A (ch1/K145A) expressed in Xenopus oocytes. Mutant ch1/K145A receptors had a reduced gating function similar to that produced by the same mutation in the wild type receptor alpha7. The mutated receptor has reduced opening rate constants, beta, and increased closing rate constants, alpha.