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Rab5-dependent autophagosome closure by ESCRT

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العنوان:	Rab5-dependent autophagosome closure by ESCRT
المؤلفون:	Jing Zhu, Hui Xu, Yanhong Xue, Rakhilya Murtazina, Liangyi Chen, Wenjing Li, Rui Li, Yongheng Liang, Haiqian Xu, Liuju Li, Zhiping Xie, Juan Cai, Ao Zhang, Mengzhu Zhao, Xiaoshuai Huang, Qunli Li, Zulin Wu, Yi Ting Zhou, Xiaoxia Cong, Nava Segev, Valeriya Gyurkovska, Dan Sun, Fan Zhou, Lei Zhao
المصدر:	Autophagy The Journal of Cell Biology
بيانات النشر:	Rockefeller University Press, 2019.
سنة النشر:	2019
مصطلحات موضوعية:	Autophagosome, Saccharomyces cerevisiae Proteins, Endosome, Endocytic cycle, Autophagy-Related Proteins, Endosomes, Saccharomyces cerevisiae, macromolecular substances, Biology, Article, ESCRT, 03 medical and health sciences, 0302 clinical medicine, Lysosome, Autophagy, medicine, Research Articles, rab5 GTP-Binding Proteins, 030304 developmental biology, 0303 health sciences, Endosomal Sorting Complexes Required for Transport, Autophagosomes, Intracellular Membranes, Cell Biology, Transport protein, Cell biology, ESCRT complex, Protein Transport, medicine.anatomical_structure, Vacuoles, Commentary, Lysosomes, 030217 neurology & neurosurgery
الوصف:	Zhou et al. identify the mechanism of autophagosome (AP) closure. They show that Rab5 GTPase regulates an interaction between the ESCRT subunit Snf7 and Atg17 to bring ESCRT to APs where it catalyzes AP closure. These findings highlight the convergence of the endocytic and autophagic pathways at this step. In the conserved autophagy pathway, autophagosomes (APs) engulf cellular components and deliver them to the lysosome for degradation. Before fusing with the lysosome, APs have to close via an unknown mechanism. We have previously shown that the endocytic Rab5-GTPase regulates AP closure. Therefore, we asked whether ESCRT, which catalyzes scission of vesicles into late endosomes, mediates the topologically similar process of AP sealing. Here, we show that depletion of representative subunits from all ESCRT complexes causes late autophagy defects and accumulation of APs. Focusing on two subunits, we show that Snf7 and the Vps4 ATPase localize to APs and their depletion results in accumulation of open APs. Moreover, Snf7 and Vps4 proteins complement their corresponding mutant defects in vivo and in vitro. Finally, a Rab5-controlled Atg17–Snf7 interaction is important for Snf7 localization to APs. Thus, we unravel a mechanism in which a Rab5-dependent Atg17–Snf7 interaction leads to recruitment of ESCRT to open APs where ESCRT catalyzes AP closure.
تدمد:	1540-8140 0021-9525
الوصول الحر:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4f388fa8467bed00c6cf9a8d6685d27Test https://doi.org/10.1083/jcb.201811173Test
حقوق:	OPEN
رقم الانضمام:	edsair.doi.dedup.....e4f388fa8467bed00c6cf9a8d6685d27
قاعدة البيانات:	OpenAIRE

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