Journal
JOURNAL OF CELL SCIENCE
Volume 132, Issue 9, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.226530
Keywords
BAR domain; Endocytosis; Clathrin-mediated endocytosis; CME; Dynamin 2; ArhGEF37
Categories
Funding
- Deutsche Forschungsgemeinschaft DFG [EXC-1003, PP-2015-08, CRC1348/A04, CRC944/P5, CRC1348/A02, CRC1348/A06]
- Medizinische Fakulta, Westfalische Wilhelms-Universitat Munster [IMF IGA-121610]
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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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