期刊
MOLECULAR PHARMACOLOGY
卷 69, 期 2, 页码 558-563出版社
AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS
DOI: 10.1124/mol.105.019356
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资金
- Medical Research Council [G118/2] Funding Source: researchfish
- MRC [G118/2] Funding Source: UKRI
- Medical Research Council [G118/2] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Much of our understanding of ligand-gated ion channels comes from heterologous expression studies. However, this technique cannot produce receptors with a predetermined subunit composition for channels formed by several different subunits and cannot insert a single mutation copy if the subunit of interest is present in several copies in the channel. Here, we describe a novel approach that overcomes these problems by expressing pentameric constructs, in which the code of the five subunits is linked ( i.e., beta 4_beta 4_alpha 3_beta 4_alpha 3). This is the first time that a concatemer of the complete pentameric receptor has been expressed for channels in the cysteine-loop superfamily. The presence of the linker did not change the agonist or antagonist sensitivity of alpha 3 beta 4 nicotinic receptors. We show evidence that the expressed receptors were made up of alpha 3 and beta 4 subunits in one pentameric fusion protein as designed in the construct. This approach can be applied to any nicotinic superfamily receptor to produce channels with a defined subunit arrangement and to introduce specific mutations at any desired location of the pentameric fusion protein.
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