Structural Determinants for Light-Dependent Membrane Binding of a Photoswitchable Polybasic Domain
文献类型：期刊论文
| 作者 | Li, Ling2,3; He, Lian1; Wu, Bo2 ; Yu, Chuandi2,3; Zhao, Hongxin2; Zhou, Yubin1; Wang, Junfeng2,3,4; Zhu, Lei2
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| 刊名 | ACS SYNTHETIC BIOLOGY
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| 出版日期 | 2021-03-19 |
| 卷号 | 10 |
| 关键词 | polybasic domain LOV2 optogenetics NMR PI(4,5)P-2 protein-lipid interaction |
| ISSN号 | 2161-5063 |
| DOI | 10.1021/acssynbio.0c00571 |
| 通讯作者 | Zhou, Yubin(yubinzhou@tamu.edu) ; Wang, Junfeng(junfeng@hmfl.ac.cn) ; Zhu, Lei(zhulei@hmfl.ac.cn) |
| 英文摘要 | OptoPB is an optogenetic tool engineered by fusion of the phosphoinositide (PI)-binding polybasic domain of Ritl (Rit-PB) to a photoreactive light-oxygen-voltage (LOV) domain. OptoPB selectively and reversibly binds the plasma membrane (PM) under blue light excitation, and in the dark, it releases back to the cytoplasm. However, the molecular mechanism of optical r egulation and lipid recognition is still unclear. Here using nuclear magnetic resonance (NMR) spectroscopy, liposome pulldown assay, and surface plasmon resonance (SPR), we find that OptoPB binds to membrane mimetics containing di- or triphosphorylated phosphatidylinositols, particularly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P-2), an acidic phospholipid predominantly located in the eukaryotic PM. In the dark, steric hindrance prevented this protein-membrane interaction, while 470 nm blue light illumination activated it. NMR titration and site-directed mutagenesis revealed that both cationic and hydrophobic Rit-PB residues are essential to the membrane interaction, indicating that OptoPB binds the membrane via a specific PI(4,5)P-2-dependent mechanism. |
| 资助项目 | National Natural Science Foundation of China[31800645] ; National Natural Science Foundation of China[U1532269] ; National Natural Science Foundation of China[21673244] ; Anhui Provincial Natural Science Foundation[18085QC65] ; Welch Foundation[BE-1913-20190330] ; American Cancer Society[RSG-16-215-01-TBE] ; High Magnetic Field Laboratory of Anhui Province |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000631444600011 |
| 出版者 | AMER CHEMICAL SOC |
| 资助机构 | National Natural Science Foundation of China ; Anhui Provincial Natural Science Foundation ; Welch Foundation ; American Cancer Society ; High Magnetic Field Laboratory of Anhui Province |
| 源URL | [http://ir.hfcas.ac.cn:8080/handle/334002/120804]  |
| 专题 | 中国科学院合肥物质科学研究院 |
| 通讯作者 | Zhou, Yubin; Wang, Junfeng; Zhu, Lei |
| 作者单位 | 1.Texas A&M Univ, Ctr Translat Canc Res, Inst Biosci & Technol, Houston, TX 77030 USA 2.Chinese Acad Sci, Hefei Inst Phys Sci, High Magnet Field Lab, CAS Key Lab High Magnet Field & Ion Beam Phys Bio, Hefei 230031, Peoples R China 3.Univ Sci & Technol China, Hefei 230026, Peoples R China 4.Anhui Univ, Inst Phys Sci & Informat Technol, Hefei 230031, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, Ling,He, Lian,Wu, Bo,et al. Structural Determinants for Light-Dependent Membrane Binding of a Photoswitchable Polybasic Domain[J]. ACS SYNTHETIC BIOLOGY,2021,10. |
| APA | Li, Ling.,He, Lian.,Wu, Bo.,Yu, Chuandi.,Zhao, Hongxin.,...&Zhu, Lei.(2021).Structural Determinants for Light-Dependent Membrane Binding of a Photoswitchable Polybasic Domain.ACS SYNTHETIC BIOLOGY,10. |
| MLA | Li, Ling,et al."Structural Determinants for Light-Dependent Membrane Binding of a Photoswitchable Polybasic Domain".ACS SYNTHETIC BIOLOGY 10(2021). |
入库方式： OAI收割
来源：合肥物质科学研究院
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