Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo

Oyinkan Olusanya, Paul D. Andrews, Jason R. Swedlow, Elizabeth Smythe (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    115 Citations (Scopus)

    Abstract

    The clathrin-coated pit is the major port of entry for many receptors and pathogens and is the paradigm for membrane-based sorting events in higher cells [1]. Recently, it has been possible to reconstitute in vitro the events leading to assembly, invagination, and budding off of clathrin-coated vesicles, allowing dissection of the machinery required for sequestration of receptors into these structures [2-6]. The AP2 adaptor complex is a key element of this machinery linking receptors to the coat lattice, and it has previously been reported that AP2 can be phosphorylated both in vitro and in vivo [7-10]. However, the physiological significance of this has never been established. Here, we show that phosphorylation of a single threonine residue (Thr156) of the μ2 subunit of the AP2 complex is essential for efficient endocytosis of transferrin both in an in vitro coated-pit budding assay and in living cells.

    Original languageEnglish
    Pages (from-to)896-900
    Number of pages5
    JournalCurrent Biology
    Volume11
    Issue number11
    DOIs
    Publication statusPublished - 5 Jun 2001

    ASJC Scopus subject areas

    • General Biochemistry,Genetics and Molecular Biology
    • General Agricultural and Biological Sciences

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