Hsp90 regulation of mitochondrial protein folding: from organelle integrity to cellular homeostasis.
Although essential for energy production and cell fate decisions, the mechanisms that govern protein homeostasis, or proteostasis, in mitochondria are only recently beginning to emerge. Fresh experimental evidence has uncovered a role of molecular chaperones of the heat shock protein 90 (Hsp90) family in overseeing the protein folding environment in mitochondria. Initially implicated in protection against cell death, there is now evidence that Hsp90-directed protein quality control in mitochondria connects to hosts of cellular homeostatic networks that become prominently exploited in human cancer.
Prostate Cancer Discovery and Development Program, The Wistar Institute Cancer Center, 3601 Spruce Street, Philadelphia, PA 19104, USA. daltieri@wistar.org
Dario C
DC
Altieri
D017209:Apoptosis; D004721:Endoplasmic Reticulum / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D033681:Mitochondrial Membrane Transport Proteins / Q000378:metabolism; D000083162:Mitochondrial Permeability Transition Pore; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D015398:Signal Transduction; D056811:Unfolded Protein Response
D018841:HSP90 Heat-Shock Proteins; D033681:Mitochondrial Membrane Transport Proteins; D000083162:Mitochondrial Permeability Transition Pore; D024101:Mitochondrial Proteins