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The anti-apoptosis ubiquitin E3 ligase XIAP promotes autophagosome-lysosome fusion during autophagy

Isabella Poetsch, Petra Ebner, Luiza Deszcz, Iris Bachtrog, Madlen Stephani, Carlos Gómez Díaz, Yasin Dagdas, View ORCID ProfileFumiyo Ikeda
doi: https://doi.org/10.1101/291294
Isabella Poetsch
1Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, 1030 Vienna, Austria
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Petra Ebner
1Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, 1030 Vienna, Austria
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Luiza Deszcz
1Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, 1030 Vienna, Austria
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Iris Bachtrog
1Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, 1030 Vienna, Austria
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Madlen Stephani
2Gregor Mendel Institute of Molecular Plant Biology GmbH (GMI), Vienna BioCenter, 1030 Vienna, Austria
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Carlos Gómez Díaz
1Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, 1030 Vienna, Austria
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Yasin Dagdas
2Gregor Mendel Institute of Molecular Plant Biology GmbH (GMI), Vienna BioCenter, 1030 Vienna, Austria
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Fumiyo Ikeda
1Institute of Molecular Biotechnology (IMBA), Vienna BioCenter, 1030 Vienna, Austria
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  • ORCID record for Fumiyo Ikeda
  • For correspondence: fumiyo.ikeda@imba.oeaw.ac.at
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Abstract

The Inhibitor of Apoptosis Protein (IAP) family members are well-known endogenous regulators of apoptosis. Whether these proteins regulate other degradation pathways is unclear. Here, we discovered that the IAP member X-linked IAP (XIAP) is crucial for macroautophagy. Loss of XIAP in mouse and human cells inhibited starvation-induced degradation of LC3 proteins and an autophagy substrate p62. It also led to the accumulation of mature autophagosomes, suggesting that XIAP controls autophagic flux by mediating autolysosome formation. Xiap∆RING/∆RING cells phenocopy the autophagy defects of Xiap−/− cells, suggesting that the ubiquitinating activity mediated by the catalytic RING domain is critical for autophagic flux. We found that XIAP physically interacts with Syntaxin 17, a regulator of autophagosome-lysosome fusion. Syntaxin 17-positive mature autophagosomes positive accumulate in the cytoplasm of starved Xiap−/− cells, suggesting that XIAP might regulate its dissociation from autophagosomes after fusion. XIAP selectively interacts with GABARAP among LC3 family members via the LIR-Docking Site (LDS). Together, our data suggest that XIAP-mediated ubiquitination regulates key autophagy regulators to promote autophagosome-lysosome fusion.

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Posted March 29, 2018.
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The anti-apoptosis ubiquitin E3 ligase XIAP promotes autophagosome-lysosome fusion during autophagy
Isabella Poetsch, Petra Ebner, Luiza Deszcz, Iris Bachtrog, Madlen Stephani, Carlos Gómez Díaz, Yasin Dagdas, Fumiyo Ikeda
bioRxiv 291294; doi: https://doi.org/10.1101/291294
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The anti-apoptosis ubiquitin E3 ligase XIAP promotes autophagosome-lysosome fusion during autophagy
Isabella Poetsch, Petra Ebner, Luiza Deszcz, Iris Bachtrog, Madlen Stephani, Carlos Gómez Díaz, Yasin Dagdas, Fumiyo Ikeda
bioRxiv 291294; doi: https://doi.org/10.1101/291294

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