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ArhGEF37 assists dynamin 2 during clathrin-mediated endocytosis.

ABSTRACT: 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)P2-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.

SUBMITTER: Viplav A

PROVIDER: S-EPMC6526708 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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ArhGEF37 assists dynamin 2 during clathrin-mediated endocytosis.

Viplav Abhiyan A Saha Tanumoy T Huertas Jan J Selenschik Philipp P Ebrahimkutty Mirsana P MP Grill David D Lehrich Julia J Hentschel Andreas A Biasizzo Monika M Mengoni Simone S Ahrends Robert R Gerke Volker V Cojocaru Vlad V Klingauf Jürgen J Galic Milos M

Journal of cell science 20190508 9

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<sub>2</sub>-depende ...[more]

PMID: 30926623

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