Open AccessArhGEF37 assists Dynamin2 during Clathrin-mediated endocytosis
Author(s) -
Abhiyan Viplav,
Tanumoy Saha,
Jan Huertas,
Philipp Selenschik,
Mirsana P. Ebrahimkutty,
David Grill,
Julia Lehrich,
Andreas Hentschel,
Monika Biasizzo,
Simone Mengoni,
Robert Ahrends,
Volker Gerke,
Vlad Cojocaru,
Jürgen Klingauf,
Milos Galic
Publication year - 2019
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.226530
Subject(s) - endocytosis , endocytic cycle , biology , clathrin , receptor mediated endocytosis , microbiology and biotechnology , function (biology) , amphiphysin , biochemistry , receptor , dynamin
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.