Molecular Chaperones as Facilitators of Protein Degradation



Molecular chaperones are widely recognized as intracellular ­folding factors. Yet, over the last couple of years more and more examples have emerged where chaperones actively participated in protein degradation. From the ­chaperone-bound state substrate proteins can be directed onto proteasome as well as autophagy-mediated degradation pathways. Chaperone-assisted degradation indeed seems to be a vital aspect of cellular protein quality control. Here we describe molecular mechanisms underlying chaperone-assisted degradation and discuss its physiological relevance in the context of neurodegenerative diseases and aging.


Ubiquitin Ligase Chaperone Activity Small Heat Shock Protein Lysosomal Degradation Ubiquitin Chain 
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© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  1. 1.Institut für ZellbiologieRheinische Friedrich-Wilhelms Universität BonnBonnGermany

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