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

内质网（ER）-质膜（PM）膜接触位点（MCS）是真核细胞内钙离子和脂质稳态的重要调节剂。In S.在酿酒酵母细胞中，6个蛋白（Ist 2，Scs 2/22和Tcb 1/2/3）的缺失显著降低了ER-PM的结合程度，表明这些蛋白是酿酒酵母中ER-PM的主要连接蛋白。啤酒。然而，这些系绳的具体功能仍然知之甚少。在这个项目中，我们解决这个问题结合功能检测与高分辨率成像ER-PM栓系在体内和体外使用冷冻电子断层扫描。

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.