Abstract
The essential cellular functions of the molecular chaperone HSP90 have been intensively investigated in fungal and mammalian model systems. Several recent publications have highlighted the importance of this chaperone complex in plant development and responsiveness to external stimuli. In particular, HSP90 is crucial for R-protein-mediated defense against pathogens. Other facets of HSP90 function in plants include its involvement in phenotypic plasticity, developmental stability, and buffering of genetic variation. Plants have emerged as powerful tools that complement other model systems in attempts to extend our knowledge of the myriad impacts of protein folding and chaperone function.
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