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PMID:16943323
Citation |
Yano, M, Nakamuta, S, Wu, X, Okumura, Y and Kido, H (2006) A novel function of 14-3-3 protein: 14-3-3zeta is a heat-shock-related molecular chaperone that dissolves thermal-aggregated proteins. Mol. Biol. Cell 17:4769-79 |
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Abstract |
The 14-3-3 proteins are highly conserved molecules that function as intracellular adaptors in a variety of biological processes, such as signal transduction, cell cycle control, and apoptosis. Here, we show that a 14-3-3 protein is a heat-shock protein (Hsp) that protects cells against physiological stress as its new cellular function. We have observed that, in Drosophila cells, the 14-3-3zeta is up-regulated under heat stress conditions, a process mediated by a heat shock transcription factor. As the biological action linked to heat stress, 14-3-3zeta interacted with apocytochrome c, a mitochondrial precursor protein of cytochrome c, in heat-treated cells, and the suppression of 14-3-3zeta expression by RNA interference resulted in the formation of significant amounts of aggregated apocytochrome c in the cytosol. The aggregated apocytochrome c was converted to a soluble form by the addition of 14-3-3zeta protein and ATP in vitro. 14-3-3zeta also resolubilized heat-aggregated citrate synthase and facilitated its reactivation in cooperation with Hsp70/Hsp40 in vitro. Our observations provide the first direct evidence that a 14-3-3 protein functions as a stress-induced molecular chaperone that dissolves and renaturalizes thermal-aggregated proteins. |
Links |
PubMed PMC1635386 Online version:10.1091/mbc.E06-03-0229 |
Keywords |
14-3-3 Proteins/chemistry; 14-3-3 Proteins/genetics; 14-3-3 Proteins/metabolism; Animals; Citrate (si)-Synthase/metabolism; Cytochromes c/metabolism; Cytosol/metabolism; Drosophila/cytology; Drosophila/metabolism; Gene Expression Regulation; HSP40 Heat-Shock Proteins/metabolism; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Response/physiology; Humans; Hyperthermia, Induced; Mitochondrial Proteins/metabolism; Molecular Chaperones/metabolism; Protein Precursors/metabolism; Protein Structure, Quaternary; Protein Transport; RNA Interference; RNA, Messenger/genetics; RNA, Messenger/metabolism; Recombinant Proteins/metabolism; Solubility; Temperature; Transcription, Genetic |
edit table |
Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
DROME:CYC1 |
located_in |
GO:0005739: mitochondrion |
ECO:0000314: direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | ||
DROME:1433Z |
involved_in |
GO:0006457: protein folding |
ECO:0000314: direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
DROME:1433Z |
involved_in |
GO:0006457: protein folding |
ECO:0000315: mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
DROME:1433Z |
involved_in |
GO:0050821: protein stabilization |
ECO:0000314: direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
DROME:1433Z |
involved_in |
GO:0050821: protein stabilization |
ECO:0000315: mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
DROME:X2J6D4 |
located_in |
GO:0005739: mitochondrion |
ECO:0000314: direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | ||
See also
References
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