SUMOylation and ubiquitination reciprocally regulate a-synuclein degradation and pathological aggreg...
SUMOylation and ubiquitination reciprocally regulate a-synuclein degradation and pathological aggregation
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Washington: National Academy of Sciences
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Language
English
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Washington: National Academy of Sciences
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a-Synuclein accumulation is a pathological hallmark of Parkinson's disease (PD). Ubiquitinated a-synuclein is targeted to proteasomal or lysosomal degradation. Here, we identify SUMOylation as a major mechanism that counteracts ubiquitination by different E3 ubiquitin ligases and regulates a-synuclein degradation. We report that PIAS2 promotes SUMO...
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SUMOylation and ubiquitination reciprocally regulate a-synuclein degradation and pathological aggregation
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TN_cdi_proquest_journals_1986946881
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1986946881
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ISSN
0027-8424
E-ISSN
1091-6490
