Journal
JOURNAL OF CELL BIOLOGY
Volume 214, Issue 5, Pages 619-635Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201602046
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Funding
- NWO Earth and Life Sciences (ALW) Open Program [822.02.014]
- Deutsche Forschungsgemeinschaft-Nederlandse Organisatie voor Wetenschappelijk Onderzoek cooperation [DN82-303]
- Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Sinergia [CRSI13_154421]
- Netherlands Organisation for Health Research and Development (ZonMW) VICI [016.130.606]
- Cancer Research UK
- Francis Crick Institute
- UK Medical Research Council
- Wellcome Trust
- Academy of Finland [265997]
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek VENI [863.13.008]
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek VICI [918.12.628]
- Deutsche Forschungsgemeinschaft [BE 4685/1-1]
- European Research Council [282333]
- Chinese Scholarship Council
- Cancer Research UK [15153] Funding Source: researchfish
- The Francis Crick Institute [10187] Funding Source: researchfish
- European Research Council (ERC) [282333] Funding Source: European Research Council (ERC)
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Autophagy is a catabolic process regulated by the orchestrated action of the autophagy-related (ATG) proteins. Recent work indicates that some of the ATG proteins also have autophagy-independent roles. Using an unbiased siRNA screen approach, we explored the extent of these unconventional functions of ATG proteins. We determined the effects of the depletion of each ATG proteome component on the replication of six different viruses. Our screen reveals that up to 36% of the ATG proteins significantly alter the replication of at least one virus in an unconventional fashion. Detailed analysis of two candidates revealed an undocumented role for ATG13 and FIP200 in picornavirus replication that is independent of their function in autophagy as part of the ULK complex. The high numbers of unveiled ATG gene-specific and pathogen specific functions of the ATG proteins calls for caution in the interpretation of data, which rely solely on the depletion of a single ATG protein to specifically ablate autophagy.
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