| Literature DB >> 32840139 |
Wayne D Hawkins1,2, Daniel J Klionsky1,2.
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.Entities:
Keywords: Autophagy; lipid transfer; lysosome; membrane protein; protein structure; stress
Year: 2020 PMID: 32840139 PMCID: PMC7595600 DOI: 10.1080/15548627.2020.1810901
Source DB: PubMed Journal: Autophagy ISSN: 1554-8627 Impact factor: 16.016