Heat shock proteins such as Hsp70 and Hsp90 have well-characterized roles as chaperones that facilitate protein folding and protect stressed cells by preventing formation of protein aggregates. They bind to unstructured or hydrophobic sequences in their targets and are regulated by co-chaperones including Hip, Hop and Cdc37. But these chaperones have another function:regulation of signal transduction. In a Commentary onp. 2809, Ellen Nollen and Richard Morimoto discuss two signalling pathways in which heat shock proteins have roles. In the Ras/Raf pathway, interactions between Raf, Hsp90 and Cdc37 seem to be required for Raf activation. The chaperone might promote Raf maturation/stability, whereas the arrival of Cdc37 could allow subsequent activation of Raf by tyrosine kinases. Chaperones are also essential in nuclear hormone receptor signalling, during which steroid aporeceptors engage in interactions with several chaperones and co-chaperones, which can stimulate or inhibit the response. Indeed, Nollen and Morimoto suggest that variations in the relative abundances of these chaperones and co-chaperones could provide a mechanism for generating cell-specific responses to intra- and extra-cellular stimuli.
Chaperones and signalling
Chaperones and signalling. J Cell Sci 15 July 2002; 115 (14): e1401. doi:
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