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    An Intrinsically Disordered Region of the Acetyltransferase p300 with Similarity to Prion-Like Domains Plays a Role in Aggregation

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    An intrinsically disordered ...
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    Genre
    Journal Article
    Date
    2012-11-01
    Author
    Kirilyuk, A
    Shimoji, M
    Catania, J
    Sahu, G
    Pattabiraman, N
    Giordano, A
    Albanese, C
    Mocchetti, I
    Toretsky, JA
    Uversky, VN
    Avantaggiati, ML
    Show allShow less
    Subject
    Alternative Splicing
    Amino Acid Sequence
    Animals
    Autophagy
    COS Cells
    Chlorocebus aethiops
    Down-Regulation
    Humans
    Lewy Bodies
    Molecular Sequence Data
    Neoplasms
    Neurodegenerative Diseases
    Oxidative Stress
    Parkinson Disease
    Prions
    Protein Denaturation
    Protein Folding
    Protein Structure, Tertiary
    Sequence Homology, Amino Acid
    alpha-Synuclein
    p300-CBP Transcription Factors
    Show allShow less
    Permanent link to this record
    http://hdl.handle.net/20.500.12613/5443
    
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    DOI
    10.1371/journal.pone.0048243
    Abstract
    Several human diseases including neurodegenerative disorders and cancer are associated with abnormal accumulation and aggregation of misfolded proteins. Proteins with high tendency to aggregate include the p53 gene product, TAU and alpha synuclein. The potential toxicity of aberrantly folded proteins is limited via their transport into intracellular sub-compartments, the aggresomes, where misfolded proteins are stored or cleared via autophagy. We have identified a region of the acetyltransferase p300 that is highly disordered and displays similarities with prion-like domains. We show that this region is encoded as an alternative spliced variant independently of the acetyltransferase domain, and provides an interaction interface for various misfolded proteins, promoting their aggregation. p300 enhances aggregation of TAU and of p53 and is a component of cellular aggregates in both tissue culture cells and in alpha-synuclein positive Lewy bodies of patients affected by Parkinson disease. Down-regulation of p300 impairs aggresome formation and enhances cytotoxicity induced by misfolded protein stress. These data unravel a novel activity of p300, offer new insights into the function of disordered domains and implicate p300 in pathological aggregation that occurs in neurodegeneration and cancer. © 2012 Kirilyuk et al.
    Citation to related work
    Public Library of Science (PLoS)
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    PLoS ONE
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    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/5425
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