Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 294, Issue 18, Pages 7128-7136Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.TM118.001190
Keywords
protein aggregation; protein misfolding; neurodegenerative disease; prion; chaperone; Prion-like protein; protein misfolding disease; protein phase separation; protein phase transition; RNA-binding protein
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Funding
- Max Planck Society
- European Research Council [725836, 643417]
- Bundesministerium fur Bildung und Forschung [01ED1601A, 031A359A]
- Joint Programme Neurodegenerative Disease (CureALS)
- European Research Council (ERC) [725836] Funding Source: European Research Council (ERC)
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Many proteins, such as RNA-binding proteins, have complex folding landscapes. How cells maintain the solubility and folding state of such proteins, particularly under stress conditions, is largely unknown. Here, we argue that prion-like low-complexity regions (LCRs) are key regulators of protein solubility and folding. We discuss emerging evidence that prion-like LCRs are not, as commonly thought, autonomous aggregation modules that adopt amyloid-like conformations, but protein-specific sequences with chaperone-like functions. On the basis of recent findings, we propose that prion-like LCRs have evolved to regulate protein phase behavior and to protect proteins against proteotoxic damage.
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