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• W2014563743 abstract "The three connexins expressed in the ocular lens each contain PDZ domain–binding motifs directing a physical association with the scaffolding protein ZO-1, but the significance of the interaction is unknown. We found that Cx50 with PDZ-binding motif mutations did not form gap junction plaques or induce cell–cell communication in HeLa cells, whereas the addition of a seven–amino acid PDZ-binding motif restored normal function to Cx50 lacking its entire C-terminal cytoplasmic domain. C-Terminal deletion had a similar although weaker effect on Cx46 but little if any effect on targeting and function of Cx43. Furthermore, small interfering RNA knockdown of ZO-1 completely inhibited the formation of gap junctions by wild-type Cx50 in HeLa cells. Thus both a PDZ-binding motif and ZO-1 are necessary for Cx50 intercellular channel formation in HeLa cells. Knock-in mice expressing Cx50 with a PDZ-binding motif mutation phenocopied Cx50 knockouts. Furthermore, differentiating lens fibers in the knock-in displayed extensive intracellular Cx50, whereas plaques in mature fibers contained only Cx46. Thus normal Cx50 function in vivo also requires an intact PDZ domain–binding motif. This is the first demonstration of a connexin-specific requirement for a connexin-interacting protein in gap junction assembly." @default.
• W2014563743 created "2016-06-24" @default.
• W2014563743 creator A5016887560 @default.
• W2014563743 creator A5016909151 @default.
• W2014563743 creator A5070309801 @default.
• W2014563743 date "2011-12-01" @default.
• W2014563743 modified "2023-09-29" @default.
• W2014563743 title "Cx50 requires an intact PDZ-binding motif and ZO-1 for the formation of functional intercellular channels" @default.
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• W2014563743 doi "https://doi.org/10.1091/mbc.e11-05-0438" @default.
• W2014563743 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3226470" @default.
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