Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes

J Cell Biol. 2020 May 4;219(5):e202001161. doi: 10.1083/jcb.202001161.

Abstract

A single particle cryo-EM reconstruction of an ∼160-kD N-terminal fragment of the lipid transport protein VPS13 reveals an ∼160-Å long channel lined with hydrophobic residues suitable for solubilizing multiple lipid fatty acid moieties. The structure suggests that VPS13 and related proteins, like the autophagy protein ATG2, can act as bridges between organelle membranes to allow bulk lipid flow between organelles.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Autophagosomes / genetics
  • Autophagosomes / ultrastructure
  • Autophagy / genetics*
  • Autophagy-Related Proteins / genetics
  • Autophagy-Related Proteins / ultrastructure*
  • Cryoelectron Microscopy
  • Endoplasmic Reticulum / genetics
  • Endoplasmic Reticulum / ultrastructure
  • Lipid Metabolism / genetics
  • Lipids / genetics
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / genetics*
  • Saccharomyces cerevisiae Proteins / ultrastructure*
  • Vesicular Transport Proteins / genetics
  • Vesicular Transport Proteins / ultrastructure*

Substances

  • ATG2 protein, S cerevisiae
  • Autophagy-Related Proteins
  • Lipids
  • Saccharomyces cerevisiae Proteins
  • VPS13 protein, S cerevisiae
  • Vesicular Transport Proteins