A Novel In Vitro CypD-Mediated p53 Aggregation Assay Suggests a Model for Mitochondrial Permeability Transition by Chaperone Systems
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- 作者：Ivan Lebedev1 ; Alice Nemajerova2 ; Zachariah H. Foda1 ; Maja Kornaj1 ; Michael Tong1 ; Ute M. Moll2 ; ute.moll@stonybrookmedicine.edu" class="auth_mail" title="E-mail the corresponding author ; Markus A. Seeliger1 ; markus.seeliger@stonybrook.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Abz-AFPF-pNA ; aminobenzoyl-Ala-Phe-Pro-Phe-4-nitroanilide ; CsA ; cyclosporine A ; CypD ; mitochondrial cyclophilin D (gene name ; PPIF ; UniProt ID ; P30405) ; GST ; glutathione S-transferase ; HSP ; heat-shock protein ; HSQC ; heteronuclear single-quantum correlation ; IR ; ischemia&ndash ; reperfusion ; MEF ; mouse embryonic fibroblast ; mPT ; mitochondrial permeability transition ; mPTP ; mitochondrial permeability transition pore ; mtUPR ; mitochondrial unfolded protein response ; OSCP ; oligomycin-sensitivity confer
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：4154-4167
- 全文大小：1474 K
文摘
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Catalytically active CypD drives insoluble aggregation of p53 in vitro.
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Active CypD causes the p53DBD to aggregate into amyloid-like fibrils in vitro.
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Inhibition of Trap1 sensitizes mouse embryonic fibroblasts to mPT in a p53-dependent manner.