High capacity of the endoplasmic reticulum to prevent secretion and aggregation of amyloidogenic proteins

Protein aggregation is associated with neurodegeneration and various other pathologies. How specific cellular environments modulate the aggregation of disease proteins is not well understood. Here, we investigated how the endoplasmic reticulum (ER) quality control system handles β‐sheet proteins tha...

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Veröffentlicht in:	The EMBO journal 2018-02, Vol.37 (3), p.337-350
Hauptverfasser:	Vincenz‐Donnelly, Lisa, Holthusen, Hauke, Körner, Roman, Hansen, Erik C, Presto, Jenny, Johansson, Jan, Sawarkar, Ritwick, Hartl, F Ulrich, Hipp, Mark S
Format:	Artikel
Sprache:	eng
Schlagworte:	Agglomeration Amyloid Amyloidogenesis Amyloidogenic Proteins - metabolism Cell Line, Tumor Chaperones Control systems Cytoplasm Cytosol Degradation EMBO20 EMBO31 EMBO32 Endoplasmic reticulum Endoplasmic Reticulum - metabolism Endoplasmic Reticulum-Associated Degradation - physiology Fibrils HEK293 Cells HeLa Cells Humans Molecular Chaperones - metabolism Neurodegeneration protein aggregation Protein Aggregation, Pathological - pathology Protein Aggregation, Pathological - prevention & control Protein Conformation, beta-Strand - physiology Protein Folding Protein interaction Proteins proteostasis Quality control RNA Interference RNA, Small Interfering - genetics Secretion Toxicity Unfolded Protein Response - physiology
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