INSERM, U1151, Institut Necker-Enfants Malades, 75015 Paris, France.
CNRS UMR 8253, Université Paris Cité, 75015 Paris, France.
Int J Mol Sci. 2022 Aug 11;23(16):8937. doi: 10.3390/ijms23168937.
Proteins interacting with CFTR and its mutants have been intensively studied using different experimental approaches. These studies provided information on the cellular processes leading to proper protein folding, routing to the plasma membrane, recycling, activation and degradation. Recently, new approaches have been developed based on the proximity labeling of protein partners or proteins in close vicinity and their subsequent identification by mass spectrometry. In this study, we evaluated TurboID- and APEX2-based proximity labeling of WT CFTR and compared the obtained data to those reported in databases. The CFTR-WT interactome was then compared to that of two CFTR (G551D and W1282X) mutants and the structurally unrelated potassium channel KCNK3. The two proximity labeling approaches identified both known and additional CFTR protein partners, including multiple SLC transporters. Proximity labeling approaches provided a more comprehensive picture of the CFTR interactome and improved our knowledge of the CFTR environment.
使用不同的实验方法，对与 CFTR 及其突变体相互作用的蛋白质进行了深入研究。这些研究提供了有关导致蛋白质正确折叠、靶向质膜、回收、激活和降解的细胞过程的信息。最近，基于蛋白质伴侣或附近蛋白质的邻近标记及其随后通过质谱法鉴定的新方法已经得到了发展。在这项研究中，我们评估了基于 TurboID 和 APEX2 的 WT CFTR 邻近标记，并将获得的数据与数据库中报告的数据进行了比较。然后，将 CFTR-WT 相互作用组与两个 CFTR（G551D 和 W1282X）突变体和结构上不相关的钾通道 KCNK3 的相互作用组进行了比较。这两种邻近标记方法鉴定了已知和额外的 CFTR 蛋白伴侣，包括多个 SLC 转运体。邻近标记方法提供了 CFTR 相互作用组更全面的图景，并提高了我们对 CFTR 环境的认识。
