Molecular crime and cellular punishment: Active detoxification of misfolded and aggregated proteins in the cell by the chaperone and protease networks

Marie Pierre Hinault, Pierre Goloubinoff*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

11 Scopus citations

Abstract

Labile or mutation-sensitised proteins may spontaneously convert into aggregation-prone conformations that may be toxic and infectious. This hazardous behavior, which can be described as a form of "molecular criminality", can be actively counteracted in the cell by a network of molecular chaperone and proteases. Similar to law enforcement agents, molecular chaperones and proteases can specifically identify, apprehend, unfold and thus neutralize "criminal" protein conformers, allowing them to subsequently refold into harmless functional proteins. Irreversibly damaged polypeptides that have lost the ability to natively refold are preferentially degraded by highly controlled ATP-consuming proteases. Damaged proteins that escape proteasomal degradation can also be "incarcerated" into dense amyloids, "evicted" from the cell, or internally "exiled" to the lysosome to be hydrolysed and recycled. Thus, remarkable parallels exist between molecular and human forms of criminality, as well as in the cellular and social responses to various forms of crime. Yet, differences also exist: whereas programmed death is the preferred solution chosen by aged and aggregation-stressed cells, collective suicide is seldom chosen by lawless societies. Significantly, there is no cellular equivalent for the role of familial care and of education in general, which is so crucial to the proper shaping of functional persons in the society. Unlike in the cell, humanism introduces a bias against radical solutions such as capital punishment, favouring crime prevention, reeducation and social reinsertion of criminals.

Original languageEnglish
Title of host publicationMolecular Aspects of the Stress Response
Subtitle of host publicationChaperones, Membranes and Networks
PublisherSpringer New York
Pages47-54
Number of pages8
ISBN (Print)9780387399744
DOIs
StatePublished - 2007
Externally publishedYes

Publication series

NameAdvances in Experimental Medicine and Biology
Volume594
ISSN (Print)0065-2598

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