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Fig. 1 | Neurological Research and Practice

Fig. 1

From: Molecular mechanisms of proteinopathies across neurodegenerative disease: a review

Fig. 1

Quality Control of Misfolded Proteins. Green arrows denote chaperone pathways. When a misfolded protein occurs, it can be detected by a molecular chaperone and refolded into a native protein. If this process cannot be completed, either because the native protein is unable to undergo further conformational change or because it has formed an aggregate, it can be sequestered and degraded at a later stage. When protein aggregates form in either an amorphous, fibrillary or oligomeric state, chaperone proteins can initiate two destruction responses. They can target them for destruction via the Ubiquitin-proteasome pathways by facilitating ubiquitin tagging, or facilitate action via BAG3/p62 them for autophagal degradation. ER = Endoplasmic Reticulum; E1 = ubiquitin–activating enzymes; E2 = ubiquitin–conjugating enzymes and E3 = ubiquitin ligases. [Based on Reference Hartl [23] and Tofaris & Buckley [52]]

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