TRAP-1, the mitochondrial Hsp90

被引：144
|
作者：
Altieri, Dario C. [1 ,2 ]
Stein, Gary S. [2 ,3 ]
Lian, Jane B. [2 ,3 ]
Languino, Lucia R. [2 ,4 ]
机构：
[1] Wistar Inst Canc Ctr, Philadelphia, PA 19104 USA
[2] Prostate Canc Discovery & Dev Program, Worcester, MA USA
[3] Univ Massachusetts, Sch Med, Dept Cell Biol, Worcester, MA 01605 USA
[4] Thomas Jefferson Univ, Kimmel Canc Ctr, Dept Canc Biol, Philadelphia, PA 19107 USA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2012年 / 1823卷 / 03期
关键词：
Mitochondria; Apoptosis; Permeability transition pore; Chaperone; Tumor growth; NECROSIS-FACTOR RECEPTOR; PERMEABILITY TRANSITION PORE; UNFOLDED PROTEIN RESPONSE; CELL-DEATH; PARKINSONS-DISEASE; OXIDATIVE STRESS; CHAPERONE TRAP1; PROSTATE-CANCER; APOPTOSIS; PINK1;
D O I：
10.1016/j.bbamcr.2011.08.007
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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). (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码：767 / 773
页数：7
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