Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly | |
Jiang, Xin2,3; Zhang, Zeting2; Cheng, Kai2; Wu, Qiong2; Jiang, Ling2,3; Pielak, Gary J.1,4,5,6; Liu, Maili2,3; Li, Conggang2,3 | |
刊名 | FASEB JOURNAL |
2019-07-01 | |
卷号 | 33期号:7页码:7985-7994 |
关键词 | prefusion state protein NMR intrinsically disordered region circular dichroism |
ISSN号 | 0892-6638 |
DOI | 10.1096/fj.201802796R |
英文摘要 | The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex comprises synaptosome-associated protein of 25 kDa (SNAP25), syntaxin-1a (syx-1), and synaptobrevin 2, which is essential for many physiologic processes requiring membrane fusion. Several studies imply that the loop region of SNAP25 plays important roles in SNARE-complex assembly. However, why and how the flexible loop facilitates the complex assembly remains poorly understood because it is purposely deleted in almost all structural studies. By using NMR spectroscopy and circular dichroism spectropolarimetry, we characterized SNAP25 structure and interactions with other SNAREs in aqueous buffer and in the membrane. We found that the N-terminal of the SNAP25 loop region binds with membrane, and this interaction induced a disorder-to-order conformational change of the loop, resulting in enhanced interaction between the C-terminal of the SNAP25 loop and syx-1. We further proved that SNARE-complex assembly efficiency decreased when we disrupted the electrostatic interaction between C-terminal of the SNAP25 loop and syx-1, suggesting that the SNAP25 loop region facilitates SNARE-complex assembly through promoting prefusion SNARE binary complex formation. Our work elucidates the role of the flexible loop and the membrane environment in SNARE-complex assembly at the residue level, which helps to understand membrane fusion, a fundamental transport and communication process in cells.-Jiang, X., Zhang, Z., Cheng, K., Wu, Q., Jiang, L., Pielak, G. J., Liu, M., Li, C. Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. |
资助项目 | Ministry of Science and Technology of China[2017YFA0505400] ; Innovation Team of Hubei Province[2016CFA002] ; National Natural Sciences Foundation of China[21735005] ; National Natural Sciences Foundation of China[21575156] ; National Natural Sciences Foundation of China[21203243] ; National Natural Sciences Foundation of China[21673284] ; K. C. Wong Education Foundation ; Chinese Academy of Sciences[QYZDJ-SSW-SLH027] |
WOS关键词 | CYSTEINE-RICH DOMAIN ; SNAP-25 ; SYNAPTOBREVIN ; PALMITOYLATION ; PHOSPHORYLATION ; ASSOCIATION ; EXOCYTOSIS ; MECHANISM ; SUGGESTS |
WOS研究方向 | Biochemistry & Molecular Biology ; Life Sciences & Biomedicine - Other Topics ; Cell Biology |
语种 | 英语 |
出版者 | FEDERATION AMER SOC EXP BIOL |
WOS记录号 | WOS:000476234700015 |
资助机构 | Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences |
内容类型 | 期刊论文 |
源URL | [http://ir.wipm.ac.cn/handle/112942/14700] |
专题 | 中国科学院武汉物理与数学研究所 |
通讯作者 | Liu, Maili; Li, Conggang |
作者单位 | 1.Univ North Carolina Chapel Hill, Lineberger Comprehens Canc Ctr, Chapel Hill, NC USA 2.Chinese Acad Sci, Natl Ctr Magnet Resonance Wuhan, Wuhan Inst Phys & Math,Wuhan Natl Lab Optoelect, Key Lab Magnet Resonance Biol Syst,State Key Lab, Wuhan 430072, Hubei, Peoples R China 3.Grad Univ Chinese Acad Sci, Beijing, Peoples R China 4.Univ North Carolina Chapel Hill, Dept Biochem & Biophys, Chapel Hill, NC USA 5.Univ North Carolina Chapel Hill, Dept Chem, Chapel Hill, NC USA 6.Univ North Carolina Chapel Hill, Integrat Program Biol & Genome Sci, Chapel Hill, NC USA |
推荐引用方式 GB/T 7714 | Jiang, Xin,Zhang, Zeting,Cheng, Kai,et al. Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly[J]. FASEB JOURNAL,2019,33(7):7985-7994. |
APA | Jiang, Xin.,Zhang, Zeting.,Cheng, Kai.,Wu, Qiong.,Jiang, Ling.,...&Li, Conggang.(2019).Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly.FASEB JOURNAL,33(7),7985-7994. |
MLA | Jiang, Xin,et al."Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly".FASEB JOURNAL 33.7(2019):7985-7994. |
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