2. Academic Validation
  3. The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance of paternal mitochondria in Caenorhabditis elegans

The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance of paternal mitochondria in Caenorhabditis elegans

  • Nat Cell Biol. 2018 Jan;20(1):81-91. doi: 10.1038/s41556-017-0008-9.
Miyuki Sato 1,  Katsuya Sato 2,  Kotone Tomura 3,  Hidetaka Kosako 4,  Ken Sato 5
Affiliations

Affiliations

  • 1 Laboratory of Molecular Membrane Biology, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan. m-sato@gunma-u.ac.jp.
  • 2 Laboratory of Molecular Membrane Biology, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan.
  • 3 Laboratory of Molecular Traffic, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan.
  • 4 Division of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima, Japan.
  • 5 Laboratory of Molecular Traffic, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma, Japan. sato-ken@gunma-u.ac.jp.
PMID: 29255173 DOI: 10.1038/s41556-017-0008-9
Abstract

In Caenorhabditis elegans embryos, paternally provided organelles, including mitochondria, are eliminated by a process of selective Autophagy called allophagy, the mechanism by which mitochondrial DNA is inherited maternally. However, it remains unclear how paternal organelles are recognized and targeted for Autophagy. Here, we identified an Autophagy receptor for allophagy, ALLO-1. ALLO-1 is essential for autophagosome formation around paternal organelles and directly binds to the worm LC3 homologue LGG-1 through its LC3-interacting region (LIR) motif. After fertilization, ALLO-1 accumulates on the paternal organelles before autophagosome formation, and this localization depends on the ubiquitin modification of the paternal organelles. We also identified IKKE-1, a worm homologue of the TBK1 and IKKε family kinase, as another critical regulator of allophagy. IKKE-1 interacts with ALLO-1, and the IKKE-1-dependent phosphorylation of ALLO-1 is important for paternal organelle clearance. Thus, we propose that ALLO-1 is the allophagy receptor whose function is regulated by IKKE-1-dependent phosphorylation.

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