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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year



Chaperone-assisted degradation: multiple paths to destruction

Nadja Kettern1 / Michael Dreiseidler1 / Riga Tawo / Jörg Höhfeld1

1Institute for Cell Biology and Bonner Forum Biomedicine, University of Bonn, Ulrich-Haberland-Str. 61a, D-53121 Bonn, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 391, Issue 5, Pages 481–489, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/bc.2010.058, March 2010

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Molecular chaperones are well known as facilitators of protein folding and assembly. However, in recent years multiple chaperone-assisted degradation pathways have also emerged, including CAP (chaperone-assisted proteasomal degradation), CASA (chaperone-assisted selective autophagy), and CMA (chaperone-mediated autophagy). Within these pathways chaperones facilitate the sorting of non-native proteins to the proteasome and the lysosomal compartment for disposal. Impairment of these pathways contributes to the development of cancer, myopathies, and neurodegenerative diseases. Chaperone-assisted degradation thus represents an essential aspect of cellular proteostasis, and its pharmacological modulation holds the promise to ameliorate some of the most devastating diseases of our time. Here, we discuss recent insights into molecular mechanisms underlying chaperone-assisted degradation in mammalian cells and highlight its biomedical relevance.

Keywords: aging; amyloid diseases; Hsp70; Hsp90; muscle weakness; ubiquitin

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