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- W2110132915 abstract "A wide range of diseases are associated with the accumulation of cytosolic protein aggregates. The effects of these aggregates on various aspects of normal cellular protein homeostasis remain to be determined. Here we find that cytosolic aggregates, without necessarily disrupting proteasome function, can markedly delay the normally rapid degradation of nontranslocated secretory and membrane protein precursors. In the case of mammalian prion protein (PrP), the nontranslocated fraction is recruited into preexisting aggregates before its triage for degradation. This recruitment permits the growth and persistence of cytosolic PrP aggregates, explaining their apparent “self-conversion” seen in earlier studies of transient proteasome inhibition. For other proteins, the aggregate-mediated delay in precursor degradation led to aggregation and/or soluble residence in the cytosol, often causing aberrant cellular morphology. Remarkably, improving signal sequence efficiency mitigated these effects of aggregates. These observations identify a previously unappreciated consequence of cytosolic aggregates for nontranslocated secretory and membrane proteins, a minor but potentially disruptive population the rapid disposal of which is critical to maintaining cellular homeostasis." @default.
- W2110132915 created "2016-06-24" @default.
- W2110132915 creator A5007776918 @default.
- W2110132915 creator A5037894071 @default.
- W2110132915 creator A5059944109 @default.
- W2110132915 date "2011-05-15" @default.
- W2110132915 modified "2023-09-27" @default.
- W2110132915 title "Cytosolic aggregates perturb the degradation of nontranslocated secretory and membrane proteins" @default.
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- W2110132915 doi "https://doi.org/10.1091/mbc.e10-07-0638" @default.
- W2110132915 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3093316" @default.
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