VDAC1型
电压依赖性阴离子通道
钙调蛋白
门控
化学
线粒体膜转运蛋白
细胞生物学
生物物理学
离子通道
细菌外膜
线粒体内膜
线粒体
生物化学
生物
受体
酶
基因
大肠杆菌
作者
T. Daniel Tuikhang Koren,Rajan Shrivastava,Shumaila Siddiqui,Subhendu Ghosh
标识
DOI:10.1021/acs.jpcb.1c10322
摘要
Calmodulin (CaM) is a key signaling protein that plays a decisive role in mitochondrial Ca2+ homeostasis and signaling and modulates the mitochondrial membrane properties. We propose that voltage-dependent anion channel 1 (VDAC1), one of the most abundant outer mitochondrial membrane (OMM) proteins, could be its possible target or site of action. VDAC1 is known to play a crucial role in the mitochondrial Ca2+ signaling mechanism. Bilayer electrophysiology experiments show that CaM significantly reduces VDAC1's conductivity and modulates its gating as well as permeability properties. Also, spectrofluorimetric analysis indicates the possibility of binding CaM with VDAC1. Theoretical analysis of fluorescence data shows that the aforementioned protein–protein interaction is not linear, but rather it is a complex nonlinear process. In VDAC1, CaM binding site has been predicted using various bioinformatics tools. It is proposed that CaM could interact with VDAC1's outer-loop region and regulate its gating properties. Our findings suggest that VDAC1–CaM interaction could play a crucial role in the transport of ions and metabolites through the OMM and the regulation of the mitochondrial Ca2+ signaling mechanism through alteration of VDAC1's gating and conductive properties.
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