期刊
EMBO JOURNAL
卷 32, 期 4, 页码 566-582出版社
WILEY
DOI: 10.1038/emboj.2013.8
关键词
ATG16L1; autophagy; TMEM59; vesicle trafficking; WD-repeat domain
资金
- Ministerio de Ciencia e Innovacion of the Spanish Government [SAF2008-00350, SAF2011-23714]
- Fundacion Solorzano, Junta de Castilla y Leon (Consejeria de Educacion) [CSI001A10-2]
- Fundacion Solorzano, Junta de Castilla y Leon (Consejeria de Sanidad)
- Consejo Superior de Investigaciones Cientificas (CSIC [200720I026]
- European Union
- FPU programme (Ministerio de Educacion, MEC, Spanish Government)
- MEC
- Social European Fund of the European Union
- EMBO
- Juan de la Cierva contract
- JAE-Doc
- Juan de la Cierva
- FPI fellowship (MEC)
Selective autophagy underlies many of the important physiological roles that autophagy plays in multicellular organisms, but the mechanisms involved in cargo selection are poorly understood. Here we describe a molecular mechanism that can target conventional endosomes for autophagic degradation. We show that the human transmembrane protein TMEM59 contains a minimal 19-amino-acid peptide in its intracellular domain that promotes LC3 labelling and lysosomal targeting of its own endosomal compartment. Interestingly, this peptide defines a novel protein motif that mediates interaction with the WD-repeat domain of ATG16L1, thus providing a mechanistic basis for the activity. The motif is represented with the same ATG16L1-binding ability in other molecules, suggesting a more general relevance. We propose that this motif may play an important role in targeting specific membranous compartments for autophagic degradation, and therefore it may facilitate the search for adaptor proteins that promote selective autophagy by engaging ATG16L1. Endogenous TMEM59 interacts with ATG16L1 and mediates autophagy in response to Staphylococcus aureus infection. The EMBO Journal (2013) 32, 566-582. doi: 10.1038/emboj.2013.8; Published online 1 February 2013
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