Heat Shock Protein 90 in Plants: Molecular Mechanisms and Roles in Stress Responses
Open Access
- 23 November 2012
- journal article
- review article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 13 (12), 15706-15723
- https://doi.org/10.3390/ijms131215706
Abstract
The heat shock protein 90 (Hsp90) family mediates stress signal transduction, and plays important roles in the control of normal growth of human cells and in promoting development of tumor cells. Hsp90s have become a currently important subject in cellular immunity, signal transduction, and anti-cancer research. Studies on the physiological functions of Hsp90s began much later in plants than in animals and fungi. Significant progress has been made in understanding complex mechanisms of HSP90s in plants, including ATPase-coupled conformational changes and interactions with cochaperone proteins. A wide range of signaling proteins interact with HSP90s. Recent studies revealed that plant Hsp90s are important in plant development, environmental stress response, and disease and pest resistance. In this study, the plant HSP90 family was classified into three clusters on the basis of phylogenetic relationships, gene structure, and biological functions. We discuss the molecular functions of Hsp90s, and systematically review recent progress of Hsp90 research in plants.This publication has 91 references indexed in Scilit:
- Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular ChaperoneMolecular Cell, 2011
- Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90Cell Death & Differentiation, 2010
- Hsp90 and co‐chaperones twist the functions of diverse client proteinsPeptide Science, 2009
- Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organismsCell Stress and Chaperones, 2009
- HSP90-buffered genetic variation is common in Arabidopsis thalianaProceedings of the National Academy of Sciences of the United States of America, 2008
- HSP90 affects the expression of genetic variation and developmental stability in quantitative traitsProceedings of the National Academy of Sciences of the United States of America, 2008
- The Mi-1-Mediated Pest Resistance Requires Hsp90 and Sgt1Plant Physiology, 2007
- An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone FunctionMolecular Cell, 2007
- Multiple Sequence Alignment Using ClustalW and ClustalXCurrent Protocols in Bioinformatics, 2002
- Hsp90 as a capacitor of phenotypic variationNature, 2002