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• W2008221108 abstract "Promyelocytic leukemia nuclear bodies (PML-NBs) comprise multiple regulatory factors and play crucial roles in the maintenance of cellular integrity, while unregulated activation of PML-NBs induces death and premature senescence. Hence, the function of PML-NBs must be directed properly; however, the mechanism that regulates PML-NBs remains unclear. In this paper, we show that PML-NBs are disintegrated by an AT-rich interaction domain family protein E2FBP1/hDril1 through specific desumoylation of promyelocytic leukemia protein (PML) in vivo and in vitro. RNA interference-mediated downregulation of E2FBP1/hDril1 results in hyperplasis of PML-NBs and consequent commitment to PML-dependent premature senescence. Thus, the function of E2FBP1/hDril1 is required for maintenance of survival potential of the cells. Our data suggest a novel mechanism to govern cellular integrity through the modulation of nuclear depots." @default.
• W2008221108 created "2016-06-24" @default.
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• W2008221108 date "2004-03-12" @default.
• W2008221108 modified "2023-10-18" @default.
• W2008221108 title "E2FBP1/hDril1 modulates cell growth through downregulation of promyelocytic leukemia bodies" @default.
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• W2008221108 doi "https://doi.org/10.1038/sj.cdd.4401412" @default.
• W2008221108 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15017387" @default.
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