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Chaperones and signalling

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 on p. 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.

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Related articles in JCS:

Chaperoning signaling pathways: molecular chaperones as stress-sensing `heat shock' proteins

Ellen A. A. Nollen and Richard I. Morimoto
JCS 2002 115: 2809-2816. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?