Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex

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Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex

Misfolded polypeptides are rapidly cleared from cells via the ubiquitin-proteasome system (UPS). However, when the UPS is impaired, misfolded polypeptides form small cytoplasmic aggregates, which are sequestered into an aggresome and ultimately degraded by aggrephagy. Despite the relevance of the aggresome to neurodegenerative proteinopathies, the molecular mechanisms underlying aggresome forma...

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Aggresomes: A Cellular Response to Misfolded Proteins

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Protein misfolding is a common event in living cells. Molecular chaperones not only assist protein folding; they also facilitate the degradation of misfolded polypeptides. When the intracellular degradative capacity is exceeded, juxtanuclear aggresomes are formed to sequester misfolded proteins. Despite the well-established role of chaperones in both protein folding and degradation, how chapero...

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Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons.

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ژورنال

عنوان ژورنال: Nature Communications

سال: 2017

ISSN: 2041-1723

DOI: 10.1038/ncomms15730