E2FBP1/hDril1 modulates cell growth through downregulation of promyelocytic leukemia bodies.

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.
Mesh Terms:
Blotting, Western, Cell Division, Cell Nucleus Structures, DNA-Binding Proteins, Down-Regulation, Escherichia coli, Fluorescein-5-isothiocyanate, Fluorescent Antibody Technique, Indirect, Fluorescent Dyes, Humans, Immunoglobulin Heavy Chains, KB Cells, Leukemia, Promyelocytic, Acute, Microscopy, Fluorescence, Nuclear Proteins, Oncogenes, Precipitin Tests, RNA, Small Interfering, Saccharomyces cerevisiae, Trans-Activators, Transcription Factors, Two-Hybrid System Techniques
Cell Death Differ.
Date: Jul. 01, 2004
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