JNK3磷酸化Bax蛋白并诱导双层脂质膜形成孔的能力

Rajeev Gupta , Subhendu Ghosh
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引用次数: 6

摘要

Bax是一种促凋亡的细胞质蛋白。在这项工作中,原生(未磷酸化)和JNK3磷酸化的Bax蛋白在人工双层膜上进行了孔形成研究。磷酸化的Bax在双层脂质膜上形成孔,而天然的Bax则不形成孔。在发生凋亡的细胞中,磷酸化的Bax形成的孔可能在细胞色素c从线粒体膜间空间释放到细胞质中起重要作用。磷酸化的Bax孔的开放状态的低电导(1.5 nS)对应的孔径为0.9 nm,这对于释放细胞色素c (~ 3.4 nm)来说是很小的。我们假设JNK3磷酸化的Bax蛋白与其他线粒体蛋白如VDAC、t-Bid等形成复合物后,形成更大的孔隙,释放细胞色素c。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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JNK3 phosphorylates Bax protein and induces ability to form pore on bilayer lipid membrane

Bax is a pro-apoptotic cytosolic protein. In this work native (unphosphorylated) and JNK3 phosphorylated Bax proteins are studied on artificial bilayer membranes for pore formation. Phosphorylated Bax formed pore on the bilayer lipid membrane whereas native one does not. In cells undergoing apoptosis the pore formed by the phosphorylated Bax could be important in cytochrome c release from the mitochondrial intermembrane space to the cytosol. The low conductance (1.5 nS) of the open state of the phosphorylated Bax pore corresponds to pore diameter of 0.9 nm which is small to release cytochrome c (∼3.4 nm). We hypothesized that JNK3 phosphorylated Bax protein can form bigger pores after forming complexes with other mitochondrial proteins like VDAC, t-Bid etc. to release cytochrome c.

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