ArhGEF37 assists dynamin 2 during clathrin-mediated endocytosis

J Cell Sci. 2019 May 8;132(9):jcs226530. doi: 10.1242/jcs.226530.

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.

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

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Clathrin-Coated Vesicles / metabolism
  • Dynamin II / metabolism*
  • Endocytosis / physiology*
  • HeLa Cells
  • Humans
  • Mice
  • NIH 3T3 Cells
  • Rho Guanine Nucleotide Exchange Factors* / chemistry
  • Rho Guanine Nucleotide Exchange Factors* / metabolism

Substances

  • Rho Guanine Nucleotide Exchange Factors
  • Dynamin II