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Dev Cell. 2015 Feb 9;32(3):304-17. doi: 10.1016/j.devcel.2014.12.011. Epub 2015 Jan 22.

A role for the ancient SNARE syntaxin 17 in regulating mitochondrial division.

Author information

1
School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan.
2
Research Institute for Science and Technology, Kogakuin University, Hachioji, Tokyo 192-0015, Japan; Informatics Program, Graduate School of Engineering, Kogakuin University, Hachioji, Tokyo 192-0015, Japan.
3
Informatics Program, Graduate School of Engineering, Kogakuin University, Hachioji, Tokyo 192-0015, Japan.
4
Department of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.
5
Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume, Fukuoka 839-0864, Japan.
6
Department of Cell Biology, University of Alberta, Edmonton, AB T6G 2H7, Canada.
7
Biomolecular Characterization Team, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
8
School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan. Electronic address: tagaya@toyaku.ac.jp.

Abstract

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 Ca(2+) homeostasis and interferes with Rab32-mediated regulation of mitochondrial 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.

PMID:
25619926
DOI:
10.1016/j.devcel.2014.12.011
[Indexed for MEDLINE]
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