Advances in understanding of the oxysterol-binding protein homologous in yeast and filamentous fungi
- 2 Downloads
Oxysterol-binding protein is an important non-vesicular trafficking protein involved in the transportation of lipids in eukaryotic cells. Oxysterol-binding protein is identified as oxysterol-binding protein-related proteins (ORPs) in mammals and oxysterol-binding protein homologue (Osh) in yeast. Research has described the function and structure of oxysterol-binding protein in mammals and yeast, but little information about the protein’s structure and function in filamentous fungi has been reported. This article focuses on recent advances in the research of Osh proteins in yeast and filamentous fungi, such as Aspergillus oryzae, Aspergillus nidulans, and Candida albicans. Furthermore, we point out some problems in the field, summarizing the membrane contact sites (MCS) of Osh proteins in yeast, and consider the future of Osh protein development.
KeywordsOxysterol-binding protein homologs Filamentous fungi Yeast Structure and function
We are grateful to the other staff of this laboratory (Hu Jianwen, Han Jizhong, Sun Yunlong, Li Haoran, Liu Mengmeng, etc.) for their other assistance in this article. The authors thank them for their long-standing support for the author’s scientific work.
Shangkun Qiu mainly participated in the data collection and article design of this article, including content writing, chapter design, and graphic design. Bin Zeng mainly provided technical support and financial assistance.
This study was financially supported by these projects in China (No.31460447, 31171731, 20142BDH80003, 2013-CXTD002, 3000035402, 00001384, 30000411, 300098020110, 300098030105, “555 talent project” of Jiangxi Province), Jiangxi Province Key Laboratory of Bioprocess Engineering, and Co-Innovation Center for In Vitro Diagnostic Reagents and Devices of Jiangxi Province.
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
- Beh CT, Cool L, Phillips J, Rine J (2001) Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 157(3):1117–1140Google Scholar
- Bosch M, Marí M, Herms A, Fernández A, Fajardo A, Kassan A, Giralt A, Colell A, Balgoma D, Barbero E, González-Moreno E, Matias N, Tebar F, Balsinde J, Camps M, Enrich C, Gross SP, García-Ruiz C, Pérez-Navarro E, Fernández-Checa JC, Pol A (2011) Caveolin-1 deficiency causes cholesterol-dependent mitochondrial dysfunction and apoptotic susceptibility. Curr Biol 21(8):681–686. https://doi.org/10.1016/j.cub.2011.03.030 Google Scholar
- Dawson PA, Van der Westhuyzen DR, Goldstein JL, Brown MS (1989) Purification of oxysterol binding protein from hamster liver cytosol. J Biol Chem 264(15):9046–9052Google Scholar
- Fukuda R, Ohta A (2013) Utilization of hydrophobic substrate by Yarrowia lipolytica. Yarrowia lipolytica :111–119. https://doi.org/10.1007/978-3-642-38320-5_5
- Fukuda R, Ohta A (2017) Enzymes for aerobic degradation of alkanes in yeasts. In: Aerobic Utilization of Hydrocarbons, Oils and Lipids. https://doi.org/10.1007/978-3-319-39782-5_7-1
- Iwama R, Kobayashi S, Ishimaru C, Ohta A, Horiuchi H, Fukuda R (2016) Functional roles and substrate specificities of twelve cytochromes P450 belonging to CYP52 family in n -alkane assimilating yeast Yarrowia lipolytica. Fungal Genet Biol 91:43–54. https://doi.org/10.1016/j.fgb.2016.03.007 Google Scholar
- Iwama R, Hara M, Mizuike A, Horiuchi H, Fukuda R (2018) Osh6p, a homologue of the oxysterol-binding protein, is involved in production of functional cytochrome P450 belonging to CYP52 family in n-alkane-assimilating yeast Yarrowia lipolytica. Biochem Biophys Res Commun 499(4):836–842. https://doi.org/10.1016/j.bbrc.2018.04.002 Google Scholar
- Johansson M, Bocher V, Lehto M, Chinetti G, Kuismanen E, Ehnholm C, Staels B, Olkkonen VM (2003) The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct. Mol Biol Cell 14(3):903–915. https://doi.org/10.1091/mbc.e02-08-0459 Google Scholar
- Keller P, Simons K (1997) Post-Golgi biosynthetic trafficking. J Cell Sci 110(Pt 24):3001Google Scholar
- Li JW, Xiao YL, Lai CF, Lou N, Ma HL, Zhu BY, Zhong WB, Yan DG (2016) Oxysterol-binding protein-related protein 4L promotes cell proliferation by sustaining intracellular Ca2+ homeostasis in cervical carcinoma cell lines. Oncotarget 7(40):65849–65861. https://doi.org/10.18632/oncotarget.11671 Google Scholar
- Quon E, Sere YY, Chauhan N, Johansen J, Sullivan DP, Dittman JS, Rice WJ, Chan RB, di Paolo G, Beh CT, Menon AK (2018) Endoplasmic reticulum-plasma membrane contact sites integrate sterol and phospholipid regulation. PLoS Biol 16(5):e2003864. https://doi.org/10.1371/journal.pbio.2003864 Google Scholar
- Raychaudhuri S, Prinz WA (2011) The diverse functions of oxysterol-binding proteins. Annu Rev Cell Dev Biol 26(1):157–177. https://doi.org/10.1146/annurev.cellbio.042308.113334 Google Scholar
- Rockenfeller P, Gourlay CW (2018) Lipotoxicty in yeast: a focus on plasma membrane signalling and membrane contact sites. FEMS Yeast Res 18(4). https://doi.org/10.1093/femsyr/foy034
- Storey MK, Byers DM, Cook HW, Ridgway ND (1998) Cholesterol regulates oxysterol binding protein (OSBP) phosphorylation and Golgi localization in Chinese hamster ovary cells: correlation with stimulation of sphingomyelin synthesis by 25-hydroxycholesterol. Biochem J 336(Pt 1):247–256. https://doi.org/10.1042/bj3360247 Google Scholar
- Takeshita N, Higashitsuji Y, Konzack S, Fischer R (2008) Apical sterol-rich membranes are essential for localizing cell end markers that determine growth directionality in the filamentous fungus aspergillus nidulans. Mol Biol Cell 19(1):339–351. https://doi.org/10.1091/mbc.e07-06-0523 Google Scholar
- Taylor FR, Shown EP, Thompson EB et al (1989) Purification, subunit structure, and DNA binding properties of the mouse oxysterol receptor. J Biol Chem 264(31):18433Google Scholar
- Tian S, Ohta A, Horiuchi H, Fukuda R (2015) Evaluation of sterol transport from the endoplasmic reticulum to mitochondria using mitochondrially targeted bacterial sterol acyltransferase in Saccharomyces cerevisiae. J Agric Chem Soc Jpn 79(10):1608–1614. https://doi.org/10.1080/09168451.2015.1058702 Google Scholar
- Tian S, Ohta A, Horiuchi H, Fukuda R (2018) Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast. J Biol Chem 293.15(2018):5636–5648. https://doi.org/10.1074/jbc.RA117.000596
- Vipond R, Bricknell IR, Durant E, Bowden TJ, Ellis AE, Smith M, MacIntyre S (1998) Defined deletion mutants demonstrate that the major secreted toxins are not essential for the virulence of Aeromonas salmonicida. Infect Immun 66(5):1990Google Scholar
- Wirtz KW, Zilversmit DB (1968) Exchange of phospholipids between liver mitochondria and microsomes in vitro. J Biol Chem 243(13):3596–3602Google Scholar
- Xu X, Bittman R, Duportail G, Heissler D, Vilcheze C, London E (2001) Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts) comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceram. J Biol Chem 276(36):33540–33546. https://doi.org/10.1074/jbc.M104776200 Google Scholar