uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Two threonine residues in the M2 segment of the alpha 1 beta 1 GABAA receptor are critical for ion channel function.
John Curtin School of Medical Research, Australian National University.
Show others and affiliations
1998 (English)In: Receptors and Channels, ISSN 1060-6823, Vol. 5, no 2, 113-24 p.Article in journal (Refereed) Published
Abstract [en]

The role of three threonine residues in the M2 hydrophobic region of the GABAA receptor has been investigated by replacing these polar residues with alanine at the 6', 10' and 13' positions of M2 in the GABAA alpha 1, and beta 1 subunits and co-expressing the mutated subunits in the baculovirus Sf9 insect cell system. GABA did not elicit a current in cells expressing either the 6' or 13' threonine to the alanine mutants. The mutant subunits formed intact heteromeric GABAA receptors as judged by the binding of [3H] muscimol or the relative level of alpha 1 protein present in the plasma membrane. In contrast, a chloride current was generated by GABA in cells expressing the 10' mutant receptor. However, the current decayed more rapidly to baseline in the continued presence of GABA in the 10' mutant receptor than in the wild type receptor. The results are discussed in terms of the possible roles of the threonine residues in the ion conduction pathway.

Place, publisher, year, edition, pages
1998. Vol. 5, no 2, 113-24 p.
National Category
URN: urn:nbn:se:uu:diva-182790PubMedID: 9606716OAI: oai:DiVA.org:uu-182790DiVA: diva2:560716
Available from: 2012-10-15 Created: 2012-10-15 Last updated: 2012-10-15

Open Access in DiVA

No full text


Search in DiVA

By author/editor
Birnir, Bryndis
In the same journal
Receptors and Channels

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 261 hits
ReferencesLink to record
Permanent link

Direct link