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- W2791631585 abstract "Recently, studies in animal models demonstrate potential roles for clathrin and AP1 in apical protein sorting in epithelial tissue. However, the precise functions of these proteins in apical protein transport remain unclear. Here, we reveal mistargeting of endogenous glycosyl phosphatidyl inositol-anchored proteins (GPI-APs) and soluble secretory proteins in Madin-Darby canine kidney (MDCK) cells upon clathrin heavy chain or AP1 subunit knockdown (KD). Using a novel directional endocytosis and recycling assay, we found that these KD cells are not only affected for apical sorting of GPI-APs in biosynthetic pathway but also for their apical recycling and basal-to-apical transcytosis routes. The apical distribution of the t-SNARE syntaxin 3, which is known to be responsible for selective targeting of various apical-destined cargo proteins in both biosynthetic and endocytic routes, is compromised suggesting a molecular explanation for the phenotype in KD cells. Our results demonstrate the importance of biosynthetic and endocytic routes for establishment and maintenance of apical localization of GPI-APs in polarized MDCK cells." @default.
- W2791631585 created "2018-03-29" @default.
- W2791631585 creator A5037368323 @default.
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- W2791631585 date "2018-02-26" @default.
- W2791631585 modified "2023-10-17" @default.
- W2791631585 title "Clathrin and AP1 are required for apical sorting of glycosyl phosphatidyl inositol‐anchored proteins in biosynthetic and recycling routes in Madin‐Darby canine kidney cells" @default.
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- W2791631585 doi "https://doi.org/10.1111/tra.12548" @default.
- W2791631585 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29352747" @default.
- W2791631585 hasPublicationYear "2018" @default.
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