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J Biol Chem. 2019 May 3;294(18):7128-7136. doi: 10.1074/jbc.TM118.001190. Epub 2018 Jun 19.

Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior.

Author information

1
From the Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
2
From the Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany alberti@mpi-cbg.de.

Abstract

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.

KEYWORDS:

Prion-like protein; RNA-binding protein; chaperone; neurodegenerative disease; prion; protein aggregation; protein misfolding; protein misfolding disease; protein phase separation; protein phase transition

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