State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, P. R. China.
University of Science and Technology of China, Hefei, Anhui 230026, P. R. China.
Anal Chem. 2021 Oct 26;93(42):14113-14120. doi: 10.1021/acs.analchem.1c02382. Epub 2021 Oct 17.
Membrane proteins tend to interact with each other in the cell membranes to form protein clusters and perform the corresponding physiological functions. However, because channel proteins are involved in many biological functions, their distribution and nano-organization in these protein clusters are unclear. To study the distribution patterns and relationships between the different channel proteins, we identified the locations of glucose transporter 1 (Glut1) and Band3 (anion transporter 1) precisely in the topography of the cytoplasmic side of the human red blood cell (hRBC) membranes using combined atomic force microscopy (AFM) and single-molecule localization microscopy (SMLM). The AFM results revealed that membrane proteins interacted with each other and aggregated into protein islands. The SMLM results showed that Glut1 and Band3 tended to form protein clusters in the hRBC membranes, and there was a strong colocalization between the two proteins. The results of the combined AFM and SMLM method indicated that the protein clusters of Glut1 and Band3 were mainly located in the protein islands of topography, and the protein islands in topography also interacted with each other to assemble into larger protein clusters or functional microdomains.
膜蛋白在细胞膜中往往相互作用，形成蛋白质簇，从而执行相应的生理功能。然而，由于通道蛋白参与许多生物功能，它们在这些蛋白质簇中的分布和纳米组织尚不清楚。为了研究不同通道蛋白的分布模式和关系，我们使用原子力显微镜（AFM）和单分子定位显微镜（SMLM）联合技术，精确确定了葡萄糖转运蛋白 1（Glut1）和阴离子转运蛋白 1（Band3）在人红细胞（hRBC）细胞膜细胞质侧拓扑结构中的位置。AFM 结果表明，膜蛋白相互作用并聚集形成蛋白质岛。SMLM 结果表明，Glut1 和 Band3 倾向于在 hRBC 膜中形成蛋白质簇，并且这两种蛋白质之间存在强烈的共定位。AFM 和 SMLM 联合方法的结果表明，Glut1 和 Band3 的蛋白质簇主要位于形貌的蛋白质岛中，形貌中的蛋白质岛也相互作用，组装成更大的蛋白质簇或功能微域。
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