SH3Ps recruit auxilin-like vesicle uncoating factors for clathrin-mediated endocytosis

Cell Rep. 2024 May 28;43(5):114195. doi: 10.1016/j.celrep.2024.114195. Epub 2024 May 7.

Abstract

Clathrin-mediated endocytosis (CME) is an essential process of cargo uptake operating in all eukaryotes. In animals and yeast, BAR-SH3 domain proteins, endophilins and amphiphysins, function at the conclusion of CME to recruit factors for vesicle scission and uncoating. Arabidopsis thaliana contains the BAR-SH3 domain proteins SH3P1-SH3P3, but their role is poorly understood. Here, we identify SH3Ps as functional homologs of endophilin/amphiphysin. SH3P1-SH3P3 bind to discrete foci at the plasma membrane (PM), and SH3P2 recruits late to a subset of clathrin-coated pits. The SH3P2 PM recruitment pattern is nearly identical to its interactor, a putative uncoating factor, AUXILIN-LIKE1. Notably, SH3P1-SH3P3 are required for most of AUXILIN-LIKE1 recruitment to the PM. This indicates a plant-specific modification of CME, where BAR-SH3 proteins recruit auxilin-like uncoating factors rather than the uncoating phosphatases, synaptojanins. SH3P1-SH3P3 act redundantly in overall CME with the plant-specific endocytic adaptor TPLATE complex but not due to an SH3 domain in its TASH3 subunit.

Keywords: BAR; CME; CP: Cell biology; SH3; SH3P; auxilin; auxilin-like; clathrin; clathrin-mediated endocytosis; endocytosis; uncoating.

MeSH terms

  • Arabidopsis Proteins* / genetics
  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / metabolism
  • Auxilins / metabolism
  • Cell Membrane / metabolism
  • Clathrin* / metabolism
  • Clathrin-Coated Vesicles / metabolism
  • Endocytosis*
  • Protein Binding
  • src Homology Domains

Substances

  • Clathrin
  • Arabidopsis Proteins
  • Auxilins