P. Csermely et al., POSSIBLE NUCLEAR FUNCTIONS OF THE MAJOR MOLECULAR CHAPERONES OF THE EUKARYOTIC CYTOPLASM, HSP90, Current Science, 74(5), 1998, pp. 442-445
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 af
ter proteotoxic stress, Hsp90, the most abundant chaperone of eukaryot
ic 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 accompany
ing steroid receptors and after cellular stress, Here we summarize our
present knowledge on the nuclear functions of Hsp90, and raise some s
uggestions for its putative role in the organization of the interphase
nucleus and mit otic chromosomes.