Identification of an intracellular microdomain of the P2X7 receptor that is crucial in basolateral membrane targeting in epithelial cells |
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Authors: | Bradley H J Liu X Collins V Owide J Goli G R Smith M Surprenant A White S J Jiang L-H |
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Institution: | a Faculty of Biological Sciences, University of Leeds, UK b Faculty of Life Science, University of Manchester, UK c Department of Physiology, Ross University School of Medicine, Commonwealth of Dominica |
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Abstract: | We investigated membrane targeting of the P2X7 receptor (P2X7R) in polarized epithelial cells using immunofluorescent confocal imaging. The wild-type receptor was targeted to the basolateral membrane, independently of adaptor protein μ1B. Deletion of the majority of the intracellular C-terminus, or the last 26 residues (P570-Y595), conferred targeting of the protein to the apical membrane. Alanine substitution in the microdomain P582-Q587 caused similar apical membrane targeting without major effect on the receptor function and surface expression. Our results show basolateral membrane targeting of the P2X7R in epithelial cells and that the intracellular C-terminal microdomain P582-Q587 is crucial in this process.Structured summaryMINT-8055849:Beta-catenin (uniprotkb:B6V8E6) and P2X7R (uniprotkb:Q64663) colocalize (MI:0403) by fluorescence microscopy (MI:0416) |
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Keywords: | P2X7 Polarized epithelial cell Basolateral domain targeting |
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