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

Sato, Miyuki, Sato, Katsuya, Tomura, Kotone, Kosako, Hidetaka, Sato, Ken·2018·Nature Cell Biology
DOI 10.1038/s41556-017-0008-9
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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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  • These probes concentrate in mitochondria due to their negative charge and react with the reduced thiols present in mitochondrial matrix proteins.

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Metadata

Authors
Sato, M., Sato, K., Tomura, K., Kosako, H., & Sato, K.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2017-12-18
Volume
20
Issue
1
Pages
81-91
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/s41556-017-0008-9
Cited by
70
References
4
Language
en
Licence
www.springer.com/tdm (unspecified)

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