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Different conformational dynamics of SNARE protein Ykt6 among yeast and mammals

文献类型： 外文期刊

作者： Ji, Jie 1 ; Yu, Yiping 1 ; Wu, Shaowen 2 ; Wang, Dongdong 3 ; Weng, Jingwei 1 ; Wang, Wenning 1 ;

作者机构： 1.Fudan Univ, Inst Biomed Sci & Multiscale Res, Inst Complex Syst, Dept Chem, Shanghai, Peoples R China

2.Guangdong Acad Agr Sci, Agro Biol Gene Res Ctr, Guangdong Key Lab Crop Germplasm Resources Preserv, Guangzhou, Guangdong, Peoples R China

3.DP Technol, Beijing, Peoples R China

期刊名称：JOURNAL OF BIOLOGICAL CHEMISTRY （ 影响因子：3.9； 五年影响因子：4.3 ）

ISSN：

年卷期： 2023 年 299 卷 8 期

页码：

收录情况： SCI

摘要： Ykt6 is one of the most conserved SNARE (N-ethylmaleimide-sensitive factor attachment protein receptor) proteins involved in multiple intracellular membrane trafficking processes. The membrane-anchoring function of Ykt6 has been elucidated to result from its conformational transition from a closed state to an open state. Two ways of regulating the conformational transition were proposed: the C-terminal lipidation and the phosphorylation at the SNARE core. Despite many aspects of common properties, Ykt6 displays differential cellular localizations and functional behaviors in different species, such as yeast, mammals, and worms. The structure- function relationship underlying these differences remains elusive. Here, we combined biochemical characterization, single-molecule FRET measurement, and molecular dynamics simulation to compare the conformational dynamics of yeast and rat Ykt6. Compared to rat Ykt6 (rYkt6), yeast Ykt6 (yYkt6) has more open conformations and could not bind dodecylphosphocholine that inhibits rYkt6 in the closed state. A point mutation T46L/Q57A was shown to be able to convert yYkt6 to a more closed and dodecylphosphocholine-bound state, where Leu46 contributes key hydrophobic interactions for the closed state. We also demonstrated that the phospho-mutation S174D could shift the conformation of rYkt6 to a more open state, but the corresponding mutation S176D in yYkt6 leads to a slightly more closed conformation. These observations shed light on the regulatory mechanism underlying the variations of Ykt6 functions across species.

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