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Chaperones: needed for both the good times and the bad times

Quinlan, R.A.; Ellis, R.J.


R.J. Ellis


In this issue, we explore the assembly roles of protein chaperones, mainly through the portal of their associated human diseases (e.g. cardiomyopathy, cataract, neurodegeneration, cancer and neuropathy). There is a diversity to chaperone function that goes beyond the current emphasis in the scientific literature on their undoubted roles in protein folding and refolding. The focus on chaperone-mediated protein folding needs to be broadened by the original Laskey discovery that a chaperone assists the assembly of an oligomeric structure, the nucleosome, and the subsequent suggestion by Ellis that other chaperones may function in assembly processes, as well as in folding. There have been a number of recent discoveries that extend this relatively neglected aspect of chaperone biology to include proteostasis, maintenance of the cellular redox potential, genome stability, transcriptional regulation and cytoskeletal dynamics. So central are these processes that we propose that chaperones stand at the crossroads of life and death because they mediate essential functions, not only during the bad times, but also in the good times. We suggest that chaperones facilitate the success of a species, and hence the evolution of individuals within populations, because of their contributions to so many key cellular processes, of which protein folding is only one.


Quinlan, R., & Ellis, R. (2013). Chaperones: needed for both the good times and the bad times. Philosophical Transactions of the Royal Society B: Biological Sciences, 368(1617), Article 20130091.

Journal Article Type Article
Publication Date May 5, 2013
Deposit Date May 1, 2014
Journal Philosophical Transactions of the Royal Society B: Biological Sciences
Print ISSN 0962-8436
Electronic ISSN 1471-2970
Publisher The Royal Society
Peer Reviewed Peer Reviewed
Volume 368
Issue 1617
Article Number 20130091
Keywords Protein chaperones, Protein folding, Human diseases, Small heat-shock proteins, Evolutionary capacitor, Assembly chaperone.