期刊
DEVELOPMENTAL CELL
卷 32, 期 3, 页码 304-317出版社
CELL PRESS
DOI: 10.1016/j.devcel.2014.12.011
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [24657141, 25291029]
- Natural Sciences and Engineering Research Council (NSERC) [386757-2010]
- NSERC [RES 0021028]
- Grants-in-Aid for Scientific Research [24570076, 26440064, 24657141, 24510156] Funding Source: KAKEN
Recent evidence suggests that endoplasmic reticulum (ER) tubules mark the sites where the GTPase Drp1 promotes mitochondrial fission via a largely unknown mechanism. Here, we show that the SNARE protein syntaxin 17 (Syn17) is present on raft-like structures of ER-mitochondria contact sites and promotes mitochondrial fission by determining Drp1 localization and activity. The hairpin-like C-terminal hydrophobic domain, including Lys-254, but not the SNARE domain, is important for this regulation. Syn17 also regulates ER Ca2+ homeostasis and interferes with Rab32-mediated regulation of mitochondria! dynamics. Starvation disrupts the Syn17-Drp1 interaction, thus favoring mitochondrial elongation during autophagy. Because we also demonstrate that Syn17 is an ancient SNARE, our findings suggest that Syn17 is one of the original key regulators for ER-mitochondria contact sites present in the last eukaryotic common ancestor. As such, Syn17 acts as a switch that responds to nutrient conditions and integrates functions for the ER and autophagosomes with mitochondrial dynamics.
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