Recent studies suggest that the chaperone function of the 90 kDa heat-shock protein, Hsp90, is restricted to help folding of nuclear hormone receptors, numerous protein kinases and damaged cytosolic proteins after proteotoxic stress. Hsp90, the most abundant chaperone of eukaryotic cytosol, may also participate in formation of cytoarchitecture and direction of cytoplasmic traffic of macromolecules. However, a small, but significant portion of Hsp90 translocates to the nucleus accompanying steroid receptors and after cellular stress. Here we summarize our present knowledge on the nuclear functions of Hsp90, and raise some suggestions for its putative role in the organization of the interphase nucleus and mitotic chromosomes.
|Number of pages||4|
|Publication status||Published - Mar 10 1998|
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