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MBC in Press, published online ahead of print August 30, 2006
Mol. Biol. Cell 10.1091/mbc.E06-03-0229

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Submitted on March 23, 2006
Revised on July 5, 2006
Accepted on August 18, 2006

A Novel Function of 14-3-3 Protein: 14-3-3{zeta} Is a Heat Shock-related Molecular Chaperone That Dissolves Thermal-aggregated Proteins

Mihiro Yano, Shinichi Nakamuta, Xueji Wu, Yuushi Okumura, and Hiroshi Kido

Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770-8503, Japan

Monitoring Editor: Jonathan Weissman

The 14-3-3 proteins are highly conserved molecules, which function as intracellular adaptors in a wide 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 that protects cells against physiological stress as its new cellular function. We have observed that, in Drosophila cells, the 14-3-3{zeta} is up-regulated under heat stress conditions, a process mediated by a heat shock transcription factor. As the biological action linked to heat stress, 14-3-3{zeta} interacted with apocytochrome c, a mitochondrial precursor protein of cytochrome c, in heat-treated cells, and the suppression of 14-3-3{zeta} expression by RNAi 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 14-3-3{zeta} protein and ATP in vitro. 14-3-3{zeta} 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. Keywords: 14-3-3 protein/cytochrome c; molecular chaperone; protein disaggregation; RNA interference

Address correspondence to: Hiroshi Kido (kido{at}ier.tokushima-u.ac.jp)






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