Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S]
Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigations. In the present study, we show that syntaxin 17...
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doaj-03763c1cc20747108800b312df5512462021-04-29T04:36:31ZengElsevierJournal of Lipid Research0022-22752018-01-01595805819Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S]Hana Kimura0Kohei Arasaki1Yuki Ohsaki2Toyoshi Fujimoto3Takayuki Ohtomo4Junji Yamada5Mitsuo Tagaya6School of Life Sciences Hachioji, Tokyo 192-0392, JapanSchool of Life Sciences Hachioji, Tokyo 192-0392, JapanDepartment of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, JapanDepartment of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, JapanSchool of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, JapanSchool of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, JapanTo whom correspondence should be addressed; School of Life Sciences Hachioji, Tokyo 192-0392, JapanLipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigations. In the present study, we show that syntaxin 17 (Stx17), a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein whose expression in the liver is regulated by diet, participates in LD biogenesis by regulating the distribution of acyl-CoA synthetase (ACSL)3, a key enzyme for LD biogenesis that redistributes from the endoplasmic reticulum (ER) to LDs during LD formation. Stx17 interacts with ACSL3, but not with LD formation-unrelated ACSL1 or ACSL4, through its SNARE domain. The interaction occurs at the ER-mitochondria interface and depends on the active site occupancy of ACSL3. Depletion of Stx17 impairs ACSL3 redistribution to nascent LDs. The defect in LD maturation due to Stx17 knockdown can be compensated for by ACSL3 overexpression, suggesting that Stx17 increases the efficiency of ACSL3 redistribution to LDs. Moreover, we show that the interaction between Stx17 and ACSL3 during LD maturation may be regulated by synaptosomal-associated protein of 23 kDa.http://www.sciencedirect.com/science/article/pii/S0022227520331163endoplasmic reticulummitochondria-associated membranesynaptosomal-associated protein of 23 kDasoluble N-ethylmaleimide-sensitive factor attachment protein receptortriacylglycerol |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Hana Kimura Kohei Arasaki Yuki Ohsaki Toyoshi Fujimoto Takayuki Ohtomo Junji Yamada Mitsuo Tagaya |
spellingShingle |
Hana Kimura Kohei Arasaki Yuki Ohsaki Toyoshi Fujimoto Takayuki Ohtomo Junji Yamada Mitsuo Tagaya Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S] Journal of Lipid Research endoplasmic reticulum mitochondria-associated membrane synaptosomal-associated protein of 23 kDa soluble N-ethylmaleimide-sensitive factor attachment protein receptor triacylglycerol |
author_facet |
Hana Kimura Kohei Arasaki Yuki Ohsaki Toyoshi Fujimoto Takayuki Ohtomo Junji Yamada Mitsuo Tagaya |
author_sort |
Hana Kimura |
title |
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S] |
title_short |
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S] |
title_full |
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S] |
title_fullStr |
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S] |
title_full_unstemmed |
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3[S] |
title_sort |
syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-coa synthetase 3[s] |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
2018-01-01 |
description |
Lipid droplets (LDs) are ubiquitous organelles that contain neutral lipids and are surrounded by a phospholipid monolayer. How proteins specifically localize to the phospholipid monolayer of the LD surface has been a matter of extensive investigations. In the present study, we show that syntaxin 17 (Stx17), a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein whose expression in the liver is regulated by diet, participates in LD biogenesis by regulating the distribution of acyl-CoA synthetase (ACSL)3, a key enzyme for LD biogenesis that redistributes from the endoplasmic reticulum (ER) to LDs during LD formation. Stx17 interacts with ACSL3, but not with LD formation-unrelated ACSL1 or ACSL4, through its SNARE domain. The interaction occurs at the ER-mitochondria interface and depends on the active site occupancy of ACSL3. Depletion of Stx17 impairs ACSL3 redistribution to nascent LDs. The defect in LD maturation due to Stx17 knockdown can be compensated for by ACSL3 overexpression, suggesting that Stx17 increases the efficiency of ACSL3 redistribution to LDs. Moreover, we show that the interaction between Stx17 and ACSL3 during LD maturation may be regulated by synaptosomal-associated protein of 23 kDa. |
topic |
endoplasmic reticulum mitochondria-associated membrane synaptosomal-associated protein of 23 kDa soluble N-ethylmaleimide-sensitive factor attachment protein receptor triacylglycerol |
url |
http://www.sciencedirect.com/science/article/pii/S0022227520331163 |
work_keys_str_mv |
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