Cellular strategies for controlling protein aggregation

• Verfasst von: Tyedmers, Jens [VerfasserIn]
• Verfasst von: Mogk, Axel [VerfasserIn]
• Verfasst von: Bukau, Bernd [VerfasserIn]
• Titel: Cellular strategies for controlling protein aggregation
• Verf.angabe: Jens Tyedmers, Axel Mogk and Bernd Bukau
• E-Jahr: 2010
• Jahr: 14 October 2010
• Umfang: 12 S.
• Fussnoten: Gesehen am 26.01.2024
• Titel Quelle: Enthalten in: Nature reviews / Molecular cell biology
• Ort Quelle: London : Macmillan, 2000
• Jahr Quelle: 2010
• Band/Heft Quelle: 11(2010), 11 vom: Nov., Seite 777-788
• ISSN Quelle: 1471-0080
• DOI: doi:10.1038/nrm2993
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Autophagy
• Sach-SW: Chaperones
• Sach-SW: Protein aggregation
• Sach-SW: Proteolysis
• K10plus-PPN: 1879064170

Abstract

Cellular systems for protein quality control act to refold or degrade misfolded proteins, thereby preventing protein aggregation. Stress conditions and ageing can lead to an exhaustion of this protective system, causing the generation of protein aggregates.The structures of protein aggregates are highly variable, ranging from amorphous to highly ordered amyloid fibrils, all of them sharing an increased β-sheet content.Cells control protein aggregation by directing misfolded proteins to distinct deposition sites.Protein aggregates are frequently segregated in an asymmetric manner during cell division, allowing the generation of damage-free daughter cells.Cells have developed different strategies to remove protein aggregates. The refolding of aggregated proteins in bacteria, yeast and plants is mediated by the cooperation of 70-kDa heat shock protein 70 (Hsp70) and Hsp104 chaperones and is facilitated by the co-aggregating of small HSPs. Aggregates can also be removed by autophagy, which is a major clearance pathway for aggregates in mammals.