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Protein Aggregation: Opposing Effects of Chaperones and Crowding

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Folding for the Synapse

Abstract

Each molecule of every protein runs the risk that at any time between its synthesis and its degradation, it will bind to one or more identical molecules to form a nonfunctional aggregate. Some protein aggregates are toxic to cells, including neurones, and are thus factors in the development of neurodegenerative and other human diseases. The incidence of such diseases is increasing, together with human longevity and obesity. The probability of protein aggregation is increased by the crowded state of most intracellular compartments, but is reduced by the activities of a diverse range of proteins acting as molecular chaperones. These chaperones use a variety of mechanisms to combat aggregation during the folding of newly synthesized protein chains, their transport into and across membranes, and their assembly into functional oligomers. This article discusses some of the key concepts and basic evidence underlying these conclusions.

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Authors and Affiliations

  1. Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK

    R. John Ellis

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  1. R. John Ellis
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Correspondence to R. John Ellis .

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Editors and Affiliations

  1. School of Biological Sciences, University of Southampton, Life Science Building (B85), SO17 1BJ, Southampton, SO16 7PX, United Kingdom

    Andreas Wyttenbach

  2. School of Biological Sciences, University of Southampton, Life Science Building (B85), SO17 1BJ, Southampton, SO16 7PX, United Kingdom

    Vincent O'Connor

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Ellis, R.J. (2011). Protein Aggregation: Opposing Effects of Chaperones and Crowding. In: Wyttenbach, A., O'Connor, V. (eds) Folding for the Synapse. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7061-9_2

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