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- W1979601948 abstract "The coxsackie and adenovirus receptor (CAR) plays key roles in epithelial barrier function at the tight junction, a localization guided in part by a tyrosine-based basolateral sorting signal, 318 YNQV 321 . Sorting motifs of this type are known to route surface receptors into clathrin-mediated endocytosis through interaction with the medium subunit (μ2) of the clathrin adaptor AP-2, but how they guide new and recycling membrane proteins basolaterally is unknown. Here, we show that YNQV functions as a canonical YxxΦ motif, with both Y318 and V321 required for the correct basolateral localization and biosynthetic sorting of CAR, and for interaction with a highly conserved pocket in the medium subunits (μ1A and μ1B) of the clathrin adaptors AP-1A and AP-1B. Knock-down experiments demonstrate that AP-1A plays a role in the biosynthetic sorting of CAR, complementary to the role of AP-1B in basolateral recycling of this receptor. Our study illustrates how two clathrin adaptors direct basolateral trafficking of a plasma membrane protein through interaction with a canonical YxxΦ motif." @default.
- W1979601948 created "2016-06-24" @default.
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- W1979601948 date "2012-02-16" @default.
- W1979601948 modified "2023-10-17" @default.
- W1979601948 title "Basolateral sorting of the coxsackie and adenovirus receptor through interaction of a canonical YXXΦ motif with the clathrin adaptors AP-1A and AP-1B" @default.
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- W1979601948 doi "https://doi.org/10.1073/pnas.1117949109" @default.
- W1979601948 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3309744" @default.
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