The anti-apoptosis ubiquitin E3 ligase XIAP promotes autophagosome-lysosome fusion during autophagy
作者： Isabella Poetsch , Petra Ebner , Luiza Deszcz , Iris Bachtrog , Madlen Stephani
DOI: 10.1101/291294
关键词:
摘要: The Inhibitor of Apoptosis Protein (IAP) family members are well-known endogenous regulators apoptosis. Whether these proteins regulate other degradation pathways is unclear. Here, we discovered that the IAP member X-linked (XIAP) crucial for macroautophagy. Loss XIAP in mouse and human cells inhibited starvation-induced LC3 an autophagy substrate p62. It also led to accumulation mature autophagosomes, suggesting controls autophagic flux by mediating autolysosome formation. XiapΔRING/ΔRING phenocopy defects Xiap-/- cells, ubiquitinating activity mediated catalytic RING domain critical flux. We found physically interacts with Syntaxin 17, a regulator autophagosome-lysosome fusion. 17-positive autophagosomes positive accumulate cytoplasm starved might its dissociation from after selectively GABARAP among via LIR-Docking Site (LDS). Together, our data suggest XIAP-mediated ubiquitination regulates key promote
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