Structure of human ATG9A: how holey art thou?

Autophagy. 2020 Nov;16(11):1929-1931. doi: 10.1080/15548627.2020.1810901. Epub 2020 Aug 25.

Abstract

Several studies have provided insight into the unique intracellular localization, dynamic trafficking and diverse repertoire of binding partners of Atg9/ATG9, but structural details of the protein have remained elusive. Guardia and colleagues now report the structure of human ATG9A to a resolution of 2.9 Å, revealing, among other features, an elaborate system of tunnels permeating the ATG9A protein complex.

Keywords: Autophagy; lipid transfer; lysosome; membrane protein; protein structure; stress.

Publication types

  • Editorial
  • Research Support, N.I.H., Extramural

MeSH terms

  • Autophagosomes / metabolism*
  • Autophagy / physiology*
  • Autophagy-Related Proteins / metabolism*
  • Humans
  • Membrane Proteins / metabolism*
  • Protein Transport / physiology
  • Vesicular Transport Proteins / metabolism*

Substances

  • ATG9A protein, human
  • Autophagy-Related Proteins
  • Membrane Proteins
  • Vesicular Transport Proteins