Plant Endocytosis Requires the ER Membrane-Anchored Proteins VAP27-1 and VAP27-3

Cell Rep. 2018 May 22;23(8):2299-2307. doi: 10.1016/j.celrep.2018.04.091.

Abstract

Through yet-undefined mechanisms, the plant endoplasmic reticulum (ER) has a critical role in endocytosis. The plant ER establishes a close association with endosomes and contacts the plasma membrane (PM) at ER-PM contact sites (EPCSs) demarcated by the ER membrane-associated VAMP-associated-proteins (VAP). Here, we investigated two plant VAPs, VAP27-1 and VAP27-3, and found an interaction with clathrin and a requirement for the homeostasis of clathrin dynamics at endocytic membranes and endocytosis. We also demonstrated direct interaction of VAP27-proteins with phosphatidylinositol-phosphate lipids (PIPs) that populate endocytic membranes. These results support that, through interaction with PIPs, VAP27-proteins bridge the ER with endocytic membranes and maintain endocytic traffic, likely through their interaction with clathrin.

Keywords: ER-PM contact sites; clathrin; endocytosis; endosplasmic reticulum; trans-golgi network.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / cytology*
  • Arabidopsis / metabolism*
  • Arabidopsis / ultrastructure
  • Arabidopsis Proteins / metabolism*
  • Cell Membrane / metabolism
  • Clathrin / metabolism
  • Endocytosis*
  • Endoplasmic Reticulum / metabolism*
  • Homeostasis
  • Lipids / chemistry
  • Membrane Proteins / metabolism*
  • Protein Binding
  • R-SNARE Proteins / metabolism*

Substances

  • Arabidopsis Proteins
  • At3g60600 protein, Arabidopsis
  • Clathrin
  • Lipids
  • Membrane Proteins
  • R-SNARE Proteins