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Updated: Jul 8, 2025

Assays for the Degradation of Misfolded Proteins in Cells
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Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

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NEMO重新塑造α-Synuclein聚合物接口,并通过与p62共同凝结起作用作为自适配器

Nikolas Furthmann1, Verian Bader1,2, Lena Angersbach1

  • 1Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany.

Nature communications
|December 19, 2023
PubMed
概括

核因素红色素2相关因子2 (NEMO) 蛋白质对于清除蛋白质聚合物至关重要,这一过程对于维持细胞蛋白质稳定和预防神经退行性疾病至关重要.

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A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model08:24

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation09:16

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相关概念视频

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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