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• W1982156058 startingPage "70" @default.
• W1982156058 abstract "In clathrin‐mediated membrane traffic, clathrin does not bind directly to cargo and instead binds to adaptors that mediate this function. For endocytosis, the main adaptor is the adaptor protein (AP)‐2 complex, but it is uncertain how clathrin contacts AP‐2. Here we tested in human cells the importance of the three binding sites that have been identified so far on the N‐terminal domain (NTD) of clathrin. We find that mutation of each of the three sites on the NTD, alone or in combination, does not block clathrin/AP‐2‐mediated endocytosis in the same way as deletion of the NTD. We report here the fourth and final site on the NTD that is required for clathrin/AP‐2‐mediated endocytic function. Each of the four interaction sites can operate alone to mediate endocytosis. The observed functional redundancy between interaction sites on the NTD explains how productivity of clathrin‐coated vesicle formation is ensured." @default.
• W1982156058 created "2016-06-24" @default.
• W1982156058 creator A5033262985 @default.
• W1982156058 creator A5074320413 @default.
• W1982156058 date "2011-10-20" @default.
• W1982156058 modified "2023-10-18" @default.
• W1982156058 title "Functional Analysis of Interaction Sites on the N-Terminal Domain of Clathrin Heavy Chain" @default.
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• W1982156058 doi "https://doi.org/10.1111/j.1600-0854.2011.01289.x" @default.
• W1982156058 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3365446" @default.
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• W1982156058 hasPublicationYear "2011" @default.
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