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Improved gating of a chimeric α7‐5HT 3A receptor upon mutations at the M2–M3 extracellular loop
Author(s) -
Castillo Mar,
Mulet José,
Bernal José Antonio,
Criado Manuel,
Sala Francisco,
Sala Salvador
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.010
Subject(s) - xenopus , gating , acetylcholine receptor , extracellular , nicotinic acetylcholine receptor , receptor , torpedo , chemistry , alpha 4 beta 2 nicotinic receptor , biophysics , microbiology and biotechnology , ion channel , trpc1 , biology , biochemistry , gene
Acetylcholine‐evoked currents of the receptor chimera α7‐5HT 3A V201 expressed in Xenopus oocytes are strikingly small when compared to the amount of α‐bungarotoxin binding sites detected at the oocyte membrane. Since the chimeric receptor is made of the extracellular N‐terminal region of the rat α7 nicotinic acetylcholine receptor and the C‐terminal region of the mouse 5‐HT 3A receptor, which includes the ion channel, we hypothesized that communication between these two regions was not optimal. Here, we show that mutating to aspartate several adjacent positions in the M2–M3 extracellular linker increases current amplitudes to different extents, thus confirming the important role of this region on receptor gating.