TRAP-1, the mitochondrial Hsp90

被引：152

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：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

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

页码：767 / 773

页数：7

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