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

Taki Nishimura, Yasunori Uchida, Rieko Yachi, Tetyana Kudlyk, Vladimir Lupashin, Takao Inoue, Tomohiko Taguchi, Hiroyuki Arai

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3534-3544
Number of pages11
JournalMolecular biology of the cell
Volume24
Issue number22
DOIs
Publication statusPublished - 2013 Nov 15
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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