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description Publicationkeyboard_double_arrow_right Article 2016 NetherlandsPublisher:Rockefeller University Press Funded by:NWO | A three-dimensional look ..., SNSF | ER-phagy mechanisms to ma..., WT +4 projectsNWO| A three-dimensional look into autophagy ,SNSF| ER-phagy mechanisms to maintain and restore endoplasmic reticulum homeostasis ,WT ,NWO| Viral strategies to evade innate antiviral host responses ,EC| XABA ,NWO| The role of autophagy in RNA virus infections ,AKA| Mechanisms in the formation of membrane structures involved in virus replicationMario Mauthe; Martijn A. Langereis; Jennifer Jung; Xingdong Zhou; Alex Jones; Wienand A. Omta; Sharon A. Tooze; Bjoern Stork; Søren R. Paludan; Tero Ahola; Dave Egan; Christian Behrends; Michal Mokry; Cornelis A. M. de Haan; Frank J. M. van Kuppeveld; Fulvio Reggiori;pmc: PMC5004442
pmid: 27573464
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. Autophagy-related (ATG) proteins regulate autophagy, but recent work indicates that some also have autophagy-independent roles. Here, Mauthe et al. perform an unbiased siRNA screen to examine the effects of ATG protein depletion on viral replication and demonstrate autophagy-independent functions for ATG13 and FIP200 in the picornaviral life cycle.
NARCIS; Utrecht Univ... arrow_drop_down Europe PubMed CentralArticle . 2016Full-Text: http://europepmc.org/articles/PMC5004442Data sources: PubMed CentralThe Journal of Cell BiologyArticle . 2016The Journal of Cell BiologyArticle . 2016 . Peer-reviewedadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1083/jcb.201602046&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess RoutesGreen hybrid 57 citations 57 popularity Top 10% influence Top 10% impulse Top 10% Powered by BIP!more_vert NARCIS; Utrecht Univ... arrow_drop_down Europe PubMed CentralArticle . 2016Full-Text: http://europepmc.org/articles/PMC5004442Data sources: PubMed CentralThe Journal of Cell BiologyArticle . 2016The Journal of Cell BiologyArticle . 2016 . Peer-reviewedadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1083/jcb.201602046&type=result"></script>'); --> </script>
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description Publicationkeyboard_double_arrow_right Article 2016 NetherlandsPublisher:Rockefeller University Press Funded by:NWO | A three-dimensional look ..., SNSF | ER-phagy mechanisms to ma..., WT +4 projectsNWO| A three-dimensional look into autophagy ,SNSF| ER-phagy mechanisms to maintain and restore endoplasmic reticulum homeostasis ,WT ,NWO| Viral strategies to evade innate antiviral host responses ,EC| XABA ,NWO| The role of autophagy in RNA virus infections ,AKA| Mechanisms in the formation of membrane structures involved in virus replicationMario Mauthe; Martijn A. Langereis; Jennifer Jung; Xingdong Zhou; Alex Jones; Wienand A. Omta; Sharon A. Tooze; Bjoern Stork; Søren R. Paludan; Tero Ahola; Dave Egan; Christian Behrends; Michal Mokry; Cornelis A. M. de Haan; Frank J. M. van Kuppeveld; Fulvio Reggiori;pmc: PMC5004442
pmid: 27573464
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. Autophagy-related (ATG) proteins regulate autophagy, but recent work indicates that some also have autophagy-independent roles. Here, Mauthe et al. perform an unbiased siRNA screen to examine the effects of ATG protein depletion on viral replication and demonstrate autophagy-independent functions for ATG13 and FIP200 in the picornaviral life cycle.
NARCIS; Utrecht Univ... arrow_drop_down Europe PubMed CentralArticle . 2016Full-Text: http://europepmc.org/articles/PMC5004442Data sources: PubMed CentralThe Journal of Cell BiologyArticle . 2016The Journal of Cell BiologyArticle . 2016 . Peer-reviewedadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1083/jcb.201602046&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euAccess RoutesGreen hybrid 57 citations 57 popularity Top 10% influence Top 10% impulse Top 10% Powered by BIP!more_vert NARCIS; Utrecht Univ... arrow_drop_down Europe PubMed CentralArticle . 2016Full-Text: http://europepmc.org/articles/PMC5004442Data sources: PubMed CentralThe Journal of Cell BiologyArticle . 2016The Journal of Cell BiologyArticle . 2016 . Peer-reviewedadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1083/jcb.201602046&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu