| http://purl.uniprot.org/citations/21832048 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21832048 | http://www.w3.org/2000/01/rdf-schema#comment | "Despite the apparent function of naturally expressed mammalian α6*-nicotinic acetylcholine receptors (α6*-nAChR; where * indicates the known or possible presence of additional subunits), their functional and heterologous expression has been difficult. Here, we report that coexpression with wild-type β3 subunits abolishes the small amount of function typically seen for all-human or all-mouse α6β4*-nAChR expressed in Xenopus oocytes. However, levels of function and agonist potencies are markedly increased, and there is atropine-sensitive blockade of spontaneous channel opening upon coexpression of α6 and β4 subunits with mutant β3 subunits harboring valine-to-serine mutations at 9'- or 13'-positions. There is no function when α6 and β2 subunits are expressed alone or in the presence of wild-type or mutant β3 subunits. Interestingly, hybrid nAChR containing mouse α6 and human (h) β4 subunits have function potentiated rather than suppressed by coexpression with wild-type hβ3 subunits and potentiated further upon coexpression with hβ3(V9'S) subunits. Studies using nAChR chimeric mouse/human α6 subunits indicated that residues involved in effects seen with hybrid nAChR are located in the α6 subunit N-terminal domain. More specifically, nAChR hα6 subunit residues Asn-143 and Met-145 are important for dominant-negative effects of nAChR hβ3 subunits on hα6hβ4-nAChR function. Asn-143 and additional residues in the N-terminal domain of nAChR hα6 subunits are involved in the gain-of-function effects of nAChR hβ3(V9'S) subunits on α6β2*-nAChR function. These studies illuminate the structural bases for effects of β3 subunits on α6*-nAChR function and suggest that unique subunit interfaces involving the complementary rather than the primary face of α6 subunits are involved."xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.263673"xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/author | "Chang Y."xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/author | "Lukas R.J."xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/author | "Dash B."xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/author | "Bhakta M."xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/pages | "37976-37989"xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/title | "Identification of N-terminal extracellular domain determinants in nicotinic acetylcholine receptor (nAChR) alpha6 subunits that influence effects of wild-type or mutant beta3 subunits on function of alpha6beta2*- or alpha6beta4*-nAChR."xsd:string |
| http://purl.uniprot.org/citations/21832048 | http://purl.uniprot.org/core/volume | "286"xsd:string |
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