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    ArhGEF37 assists dynamin 2 during clathrin-mediated endocytosis

    Year: 2019

    Journal: J. Cell Sci., Volume 132, MAY

    Authors: Viplav, Abhiyan; Saha, Tanumoy; Huertas, Jan; Selenschik, Philipp; Ebrahimkutty, Mirsana P.; Grill, David; Lehrich, Julia; Hentschel, Andreas; Biasizzo, Monika; Mengoni, Simone; Ahrends, Robert; Gerke, Volker; Cojocaru, Vlad; Klingauf, Juergen; Galic, Milos

    Keywords: BAR domain; Endocytosis; Clathrin-mediated endocytosis; CME; Dynamin 2; ArhGEF37

    Clathrin-mediated endocytosis (CME) engages over 30 proteins to secure efficient cargo and membrane uptake. While the function of most core CME components is well established, auxiliary mechanisms crucial for fine-tuning and adaptation remain largely elusive. In this study, we identify ArhGEF37, a currently uncharacterized protein, as a constituent of CME. Structure prediction together with quantitative cellular and biochemical studies present a unique BAR domain and PI(4,5)P-2-dependent protein-membrane interactions. Functional characterization yields accumulation of ArhGEF37 at dynamin 2-rich late endocytic sites and increased endocytosis rates in the presence of ArhGEF37. Together, these results introduce ArhGEF37 as a regulatory protein involved in endocytosis.
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