Structural determinants of ER-plasma membrane contact site function (P22)

内质网(ER)-质膜(PM)膜接触点(MCS)是真核细胞内钙离子和脂质稳态的重要调节器。在酿酒酵母细胞中，6种蛋白质(Ist2、Scs2/22和Tcb1/2/3)的缺失显著降低了ER-PM结合的程度，表明这些蛋白质是酿酒酵母ER-PM的主要纽带。然而，这些系绳的具体功能仍然知之甚少。在这个项目中，我们使用冷冻电子断层扫描技术，将功能分析与体内和体外ER-PM系链的高分辨率成像相结合来解决这一问题。

Endoplasmic reticulum (ER)-plasma membrane (PM) membrane contact sites (MCS) are critical modulators of Ca2+ and lipid homeostasis in eukaryotic cells. In S. cerevisiae cells, the deletion of six proteins (Ist2, Scs2/22 and Tcb1/2/3) dramatically reduces the extent of ER-PM association, indicating that these proteins are the main ER-PM tethers in S. cerevisiae. However, the specific functions of these tethers remain poorly understood. In this project, we address this issue combining functional assays with high resolution imaging of ER-PM tethers in vivo and in vitro using cryo-electron tomography.