To be, or not to be--molecular chaperones in protein degradation.
To be, or not to be--that is the question not only for Hamlet in Shakespeare's drama but also for a protein associated with molecular chaperones. While long viewed exclusively as cellular folding factors, molecular chaperones recently emerged as active participants in protein degradation. This places chaperones at the center of a life or death decision during protein triage. Here we highlight molecular mechanisms that underlie chaperone action at the folding/degradation interface in mammalian cells. We discuss the importance of chaperone-assisted degradation for the regulation of cellular processes and its emerging role as a target for therapeutic intervention in cancer and amyloid diseases.
Arndt
V
V
Institut für Zellbiologie, Rheinische Friedrich Wilhelms-Universität Bonn, Ulrich-Haberland-Str. 61a, 53121, Bonn, Germany.
Rogon
C
C
Höhfeld
J
J
D000818:Animals; D017209:Apoptosis; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D009369:Neoplasms; D019636:Neurodegenerative Diseases; D011489:Protein Denaturation; D011506:Proteins / Q000378:metabolism*; D025801:Ubiquitin
D018832:Molecular Chaperones; D011506:Proteins; D025801:Ubiquitin