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Advances in understanding of the oxysterol-binding protein homologous in yeast and filamentous fungi

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Abstract

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.

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Acknowledgements

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.

Funding

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.

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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.

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Correspondence to Bin Zeng.

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Qiu, S., Zeng, B. Advances in understanding of the oxysterol-binding protein homologous in yeast and filamentous fungi. Int Microbiol 22, 169–179 (2019). https://doi.org/10.1007/s10123-019-00056-6

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  • DOI: https://doi.org/10.1007/s10123-019-00056-6

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