Roh Jae Won, Choi Hye Won, Gee Heon Yung
Department of Pharmacology, Graduate School of Medical Science, Brain Korea 21 Project, Yonsei University College of Medicine, Seoul 03722, Republic of Korea; Woo Choo Lee Institute for Precision Drug Development, Seoul 03722, Republic of Korea.
Division of Life Sciences, College of Life Sciences and Biotechnology, Korea University, Seoul 02841, Republic of Korea.
Mol Cells. 2025 Feb;48(2):100174. doi: 10.1016/j.mocell.2024.100174. Epub 2024 Dec 28.
Plasma membrane proteins are crucial for signal transduction, trafficking, and cell-cell interactions, all of which are vital for cell survival. These proteins, including G-protein coupled receptors, ion channels, transporters, and receptors, are key drug targets due to their central role in receiving and amplifying cellular signals. However, the isolation and purification of plasma membrane proteins pose significant challenges because of their integration with phospholipid bilayers and the small fraction of these proteins present in the plasma membrane. Biotinylation, in combination with streptavidin beads, provides an effective method for surface protein analysis by specifically labeling surface proteins without penetrating the cell membrane, enabling precise isolation and analysis with minimal contamination. In this study, we describe a 1-step method for analyzing plasma membrane proteins that can be routinely implemented in many laboratories.
质膜蛋白对于信号转导、运输以及细胞间相互作用至关重要,所有这些对于细胞存活都至关重要。这些蛋白质,包括G蛋白偶联受体、离子通道、转运蛋白和受体,由于它们在接收和放大细胞信号中起核心作用,所以是关键的药物靶点。然而,质膜蛋白的分离和纯化面临重大挑战,因为它们与磷脂双层整合,且在质膜中所占比例较小。生物素化结合链霉亲和素磁珠,通过特异性标记表面蛋白而不穿透细胞膜,为表面蛋白分析提供了一种有效方法,能够以最小的污染进行精确分离和分析。在本研究中,我们描述了一种可在许多实验室常规实施的分析质膜蛋白的一步法。