The V-ATPase complex regulates non-canonical Atg8-family protein lipidation through ATG16L1 recruitment

Autophagy. 2022 Mar;18(3):707-708. doi: 10.1080/15548627.2022.2029233. Epub 2022 Mar 8.

Abstract

Conjugation of the Atg8 (autophagy related 8) family of ubiquitin-like proteins to phospholipids of the phagophore is a hallmark of macroautophagy/autophagy. Consequently, Atg8 family members, especially LC3B, are commonly used as a marker of autophagosomes. However, the Atg8 family of proteins are not found solely attached to double-membrane autophagosomes. In non-canonical Atg8-family protein lipidation they become conjugated to single membranes. We have shown that this process is triggered by recruitment of ATG16L1 by the vacuolar-type H+-translocating ATPase (V-ATPase) proton pump, suggesting a role for pH sensing in recruitment of Atg8-family proteins to single membranes.

Keywords: ATG16L1; Atg4; Atg8; CASM; SopF; V-ATPase; influenza; lipidation; non-canonical autophagy.

MeSH terms

  • Autophagy*
  • Autophagy-Related Protein 8 Family* / metabolism
  • Autophagy-Related Proteins* / metabolism
  • Humans
  • Microtubule-Associated Proteins* / metabolism
  • Proton-Translocating ATPases* / metabolism

Substances

  • ATG16L1 protein, human
  • Autophagy-Related Protein 8 Family
  • Autophagy-Related Proteins
  • GABARAPL2 protein, human
  • Microtubule-Associated Proteins
  • Proton-Translocating ATPases