TRAP-1, the mitochondrial Hsp90

TRAP-1, the mitochondrial Hsp90

Protein folding quality control does not occur randomly in cells, but requires the action of specialized molecular chaperones compartmentalized in subcellular microenvironments and organelles. Fresh experimental evidence has now linked a mitochondrial-specific Heat Shock Protein-90 (Hsp90) homolog, Tumor Necrosis Factor Receptor-Associated Protein-1 (TRAP-1) to pleiotropic signaling circuitries of organelle integrity and cellular homeostasis. TRAP-1-directed compartmentalized protein folding is broadly exploited in cancer and neurodegenerative diseases, presenting new opportunities for therapeutic intervention in humans. This article is part of a Special Issue entitled: Heat Shock Protein 90 (Hsp90).► TRAP-1 is a mitochondrial-specific Hsp90 chaperone. ► Antagonizes mitochondrial apoptosis and oxidative stress. ► Regulates the mitochondrial permeability transition pore. ► Controls the protein folding environment in mitochondria. ► Couples to the cellular stress response and gene expression.

蛋白质折叠质量控制在细胞内并非随机发生，而是需要位于亚细胞微环境和细胞器中的特异性分子伴侣发挥作用。新的实验证据现已将一种线粒体特异性热休克蛋白 - 90（Hsp90）同源物，即肿瘤坏死因子受体相关蛋白 - 1（TRAP - 1）与细胞器完整性和细胞内稳态的多效性信号通路联系起来。由TRAP - 1引导的区室化蛋白质折叠在癌症和神经退行性疾病中被广泛利用，为人类的治疗干预提供了新的机会。本文是题为《热休克蛋白90（Hsp90）》特刊的一部分。 ► TRAP - 1是一种线粒体特异性Hsp90伴侣蛋白。 ► 拮抗线粒体凋亡和氧化应激。 ► 调节线粒体通透性转换孔。 ► 控制线粒体中的蛋白质折叠环境。 ► 与细胞应激反应和基因表达相偶联。