Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation
- National Institute of Biological Sciences, China
Abstract
Autophagy is a proteolytic pathway conserved from yeasts to mammals. Atg1 kinase is essential for autophagy but how its activity is controlled remains insufficiently understood. Here, we show that, in the fission yeast Schizosaccharomyces pombe, Atg1 kinase activity requires Atg11, the ortholog of mammalian FIP200/RB1CC1, but does not require Atg13, Atg17, or Atg101. Remarkably, a 62-amino-acid region of Atg11 is sufficient for the autophagy function of Atg11 and for supporting the Atg1 kinase activity. This region harbors an Atg1-binding domain and a homodimerization domain. Dimerizing Atg1 is the main role of Atg11, as it can be bypassed by artificially dimerizing Atg1. In an Atg1 dimer, only one Atg1 molecule needs to be catalytically active, suggesting that Atg1 activation can be achieved through cis-autophosphorylation. We propose that mediating Atg1 oligomerization and activation may be a conserved function of Atg11/FIP200 family proteins and cis-autophosphorylation may be a general mechanism of Atg1 activation.
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All data generated or analysed during this study are included in the manuscript and supporting files.
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Funding
National Basic Research Program of China (2014CB849901)
- Li-Lin Du
National Basic Research Program of China (2014CB849801)
- Meng-Qiu Dong
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2020, Pan et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation
eLife 9:e58073.
https://doi.org/10.7554/eLife.58073
