TAILIEUCHUNG - Báo cáo khoa học: Tyrosine-dependent basolateral targeting of human connexin43–eYFP in Madin–Darby canine kidney cells can be disrupted by the oculodentodigital dysplasia mutation L90V

Polarized membrane sorting of connexin 43 (Cx43) has not been well-char-acterized. Based on the presence of a putative sorting signal, YKLV(286– 289), within its C-terminal cytoplasmic domain, we hypothesized that Cx43 is selectively expressed on the basolateral surface of Madin–Darby canine kidney (MDCK) cells in a tyrosine-dependent manner. | Tyrosine-dependent basolateral targeting of human connexin43-eYFP in Madin-Darby canine kidney cells can be disrupted by the oculodentodigital dysplasia mutation L90V Jana Chtchetinin1 2 Wes D. Gifford1 2 Sichen Li1 2 William A. Paznekas3 Ethylin Wang Jabs3 4 and Albert Lai1 2 1 Department of Neurology David Geffen Schoolof Medicine at UCLA Los Angeles CA USA 2 Henry E. Singleton Brain Cancer Research Program David Geffen Schoolof Medicine at UCLA Los Angeles CA USA 3 Institute of Genetic Medicine Johns Hopkins University Baltimore MD USA 4 Department of Genetics and Genomic Sciences Mount Sinai Schoolof Medicine New York NY USA Keywords basolateral connexin43 oculodentodigital dysplasia tyrosine Correspondence A. Lai 710 Westwood Plaza Suite 1-230 Reed Neurological Research Center Los Angeles CA 90095 USA Fax 1 310 825 0644 Tel 1 310 825 5321 E-mail albertlai@ Received 10 February 2009 revised 16 September 2009 accepted 25 September 2009 doi Polarized membrane sorting of connexin 43 Cx43 has not been well-characterized. Based on the presence of a putative sorting signal YKLV 286-289 within its C-terminal cytoplasmic domain we hypothesized that Cx43 is selectively expressed on the basolateral surface of Madin-Darby canine kidney MDCK cells in a tyrosine-dependent manner. We generated stable MDCK cell lines expressing human wild-type and mutant Cx43-eYFP and analyzed the membrane localization of Cx43-eYFP within polarized monolayers using confocal microscopy and selective surface biotinylation. We found that wild-type Cx43-eYFP was selectively targeted to the basolateral membrane domain of MDCK cells. Substitution of alanine for Y286 disrupted basolateral targeting of Cx43-eYFP. Additionally substitution of a sequence containing the transferrin receptor internalization signal LSYTRF for PGYKLV 284-289 also disrupted basolateral targeting. Taken together these results indicate that Y286 in its native amino acid sequence

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