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Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs

Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) have been implicated in the distribution of sterols among intracellular organelles. OSBP regulates the Golgi cholesterol level, but how it relates to Golgi function is elusive. Here we report that OSBP is essential for the localizatio...

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Autores principales: Nishimura, Taki, Uchida, Yasunori, Yachi, Rieko, Kudlyk, Tetyana, Lupashin, Vladimir, Inoue, Takao, Taguchi, Tomohiko, Arai, Hiroyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3826991/
https://www.ncbi.nlm.nih.gov/pubmed/24048449
http://dx.doi.org/10.1091/mbc.E13-05-0250
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author Nishimura, Taki
Uchida, Yasunori
Yachi, Rieko
Kudlyk, Tetyana
Lupashin, Vladimir
Inoue, Takao
Taguchi, Tomohiko
Arai, Hiroyuki
author_facet Nishimura, Taki
Uchida, Yasunori
Yachi, Rieko
Kudlyk, Tetyana
Lupashin, Vladimir
Inoue, Takao
Taguchi, Tomohiko
Arai, Hiroyuki
author_sort Nishimura, Taki
collection PubMed
description Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) have been implicated in the distribution of sterols among intracellular organelles. OSBP regulates the Golgi cholesterol level, but how it relates to Golgi function is elusive. Here we report that OSBP is essential for the localization of intra-Golgi soluble vesicle N-ethylmaleimide-sensitive fusion attachment protein receptors (v-SNAREs). Depletion of OSBP by small interfering RNA causes mislocalization of intra-Golgi v-SNAREs GS28 and GS15 throughout the cytoplasm without affecting the perinuclear localization of Golgi target-SNARE syntaxin5 and reduces the abundance of a Golgi enzyme, mannosidase II (Man II). GS28 mislocalization and Man II reduction are also induced by cellular cholesterol depletion. Three domains of OSBP—an endoplasmic reticulum–targeting domain, a Golgi-targeting domain, and a sterol-binding domain—are all required for Golgi localization of GS28. Finally, GS28 mislocalization and Man II reduction in OSBP-depleted cells are largely restored by depletion of ArfGAP1, a regulator of the budding of coat protein complex (COP)-I vesicles. From these results, we postulate that Golgi cholesterol level, which is controlled by OSBP, is essential for Golgi localization of intra-Golgi v-SNAREs by ensuring proper COP-I vesicle transport.
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spelling pubmed-38269912014-01-30 Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs Nishimura, Taki Uchida, Yasunori Yachi, Rieko Kudlyk, Tetyana Lupashin, Vladimir Inoue, Takao Taguchi, Tomohiko Arai, Hiroyuki Mol Biol Cell Articles Oxysterol-binding protein (OSBP) and OSBP-related proteins (ORPs) have been implicated in the distribution of sterols among intracellular organelles. OSBP regulates the Golgi cholesterol level, but how it relates to Golgi function is elusive. Here we report that OSBP is essential for the localization of intra-Golgi soluble vesicle N-ethylmaleimide-sensitive fusion attachment protein receptors (v-SNAREs). Depletion of OSBP by small interfering RNA causes mislocalization of intra-Golgi v-SNAREs GS28 and GS15 throughout the cytoplasm without affecting the perinuclear localization of Golgi target-SNARE syntaxin5 and reduces the abundance of a Golgi enzyme, mannosidase II (Man II). GS28 mislocalization and Man II reduction are also induced by cellular cholesterol depletion. Three domains of OSBP—an endoplasmic reticulum–targeting domain, a Golgi-targeting domain, and a sterol-binding domain—are all required for Golgi localization of GS28. Finally, GS28 mislocalization and Man II reduction in OSBP-depleted cells are largely restored by depletion of ArfGAP1, a regulator of the budding of coat protein complex (COP)-I vesicles. From these results, we postulate that Golgi cholesterol level, which is controlled by OSBP, is essential for Golgi localization of intra-Golgi v-SNAREs by ensuring proper COP-I vesicle transport. The American Society for Cell Biology 2013-11-15 /pmc/articles/PMC3826991/ /pubmed/24048449 http://dx.doi.org/10.1091/mbc.E13-05-0250 Text en © 2013 Nishimura et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Nishimura, Taki
Uchida, Yasunori
Yachi, Rieko
Kudlyk, Tetyana
Lupashin, Vladimir
Inoue, Takao
Taguchi, Tomohiko
Arai, Hiroyuki
Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
title Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
title_full Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
title_fullStr Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
title_full_unstemmed Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
title_short Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs
title_sort oxysterol-binding protein (osbp) is required for the perinuclear localization of intra-golgi v-snares
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3826991/
https://www.ncbi.nlm.nih.gov/pubmed/24048449
http://dx.doi.org/10.1091/mbc.E13-05-0250
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