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.
KeywordsUbiquitin Ligase Chaperone Activity Small Heat Shock Protein Lysosomal Degradation Ubiquitin Chain
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