Molecular cloning and characterization of a novel human variant of RIC-3, a putative chaperone of nicotinic acetylcholine receptors
Résumé
Recent reports demonstrate that the RIC-3 protein is important for the maturation of nicotinic acetylcholine receptors. In the present work RIC-3e, a novel variant of RIC-3 is described. This variant carries a deletion of exons 4 and 5 resulting in a protein product lacking a conserved coiled-coil domain. Like RIC-3, the new variant is predominantly but not exclusively expressed in the brain. The analysis of expression of RIC-3 variants' mRNA and of α7-nAChR mRNA in a set of human tissues shows a similar profile. The RIC-3e protein is functionally active and enables surface expression of mature α7-nAChRs in cell lines otherwise not permissive for the expression of this receptor.
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