A sequence motif responsible for ER export and surface expression of Kir2.0 inward rectifier K+ channels

AbstractIntegral membrane proteins are sorted via the secretory pathway. It was proposed that this pathway is non-selective provided that the cargo protein is properly assembled and lacks an endoplasmic reticulum (ER) retention signal. However, recent experimental evidence suggests that efficient export of proteins from the ER to the Golgi complex is not simply a default pathway. Here we demonstrate a novel sequence motif (FxYENEV) in the cytoplasmic C-terminus of mammalian inward rectifier potassium (Kir) channels which determines ER export. This motif is found to be both necessary and sufficient for efficient export from the ER that eventually leads to efficient surface expression of Kir2.1 channels

Desensitization of the P2X2 receptor controlled by alternative splicing

AbstractP2X receptors are ion channels gated by extracellular ATP. We report here cloning of a P2X2 receptor splice variant (P2X2-2) carrying a 207 bp deletion in the intracellular C-terminus and the analysis of the corresponding genomic structure of the P2X2 gene. P2X2-2 is as highly expressed as the original P2X2 sequence in various tissues. ATP-activated currents mediated by heterologous expressed P2X2 or P2X2-2 receptors showed significant differences in desensitization time constants and steady-state currents in the continuous presence of ATP. These results imply functional differences between cells differentially expressing these P2X2 isoforms.©1997 Federation of European Biochemical Societies