Abstract
Although there is a high degree of homology in the M2 transmembrane segments of alpha1 and beta1 subunits, subunit-specific effects were observed in alpha1beta1 GABA(A) receptors expressed in Spodoptera frugipedra (Sf9) cells when the conserved 13' threonine residue in the M2 transmembrane region was mutated to alanine. When threonine 263 (13') was mutated to alanine in the beta1 subunit, high-affinity muscimol binding and the response to GABA were abolished. This did not occur when the threonine 263 (13') was mutated to alanine in the alpha1 subunit, but the rate of desensitisation increased and the effect of bicuculline, a competitive inhibitor, was reduced. The results show differential effects of subunits on receptor function and support a role for M2 in desensitisation.
Original language | English |
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Pages (from-to) | 345-348 |
Journal | European Journal of Pharmacology |
Volume | 370 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1999 |
Externally published | Yes |
Bibliographical note
The information about affiliations in this record was updated in December 2015.The record was previously connected to the following departments: GABA Channels in Physiology and Pharmacology (013241570)
Subject classification (UKÄ)
- Pharmacology and Toxicology
Free keywords
- M2 transmembrane segment
- Ligand-gated
- GABAA receptor
- human
- Sf9 cell
- Desensitization
- Receptor assembly