An essential role for the ATG8 ortholog LC3C in antibacterial autophagy

Natalia Von Muhlinen, Masato Akutsu, Benjamin J. Ravenhil, Ágnes Foeglein, Stuart Bloor, Trevor J. Rutherford, Stefan M.V. Freund, David Komander, Felix Randow

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Autophagy defends the mammalian cytosol against bacterial invasion. Efficient bacterial engulfment by autophagy requires cargo receptors that bind (a) homolog(s) of the ubiquitinlike protein Atg8 on the phagophore membrane. The existence of multiple ATG8 orthologs in higher eukaryotes suggests that they may perform distinct functions. However, no specific role has been assigned to any mammalian ATG8 ortholog. We recently discovered that the autophagy receptor CALCOCO2/ NDP52, which detects cytosolinvading Salmonella enterica serovar Typhimurium (S. Typhimurium), preferentially binds LC3C. The CALCOCO2/ NDP52-LC3C interaction is essential for cell-autonomous immunity against cytosol- exposed S. Typhimurium, because cells lacking either protein fail to target bacteria into the autophagy pathway. The selectivity of CALCOCO2/ NDP52 for LC3C is determined by a novel LC3C interacting region (CLIR), in which the lack of the key aromatic residue of canonical LIRs is compensated by LC3C-specific interactions. Our findings provide a new layer of regulation to selective autophagy, suggesting that specific interactions between autophagy receptors and the ATG8 orthologs are of biological importance.

Original languageEnglish
Pages (from-to)784-786
Number of pages3
JournalAutophagy
Volume9
Issue number5
DOIs
Publication statusPublished - 2013 May
Externally publishedYes

Keywords

  • ATG8/LC3
  • Autophagy
  • LC3C
  • LIR
  • NDP52
  • Salmonella

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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