Abstract
TRAF and TNF receptor-associated protein (TTRAP) is a multifunctional protein that can act in the nucleus as a 5'-tyrosyl DNA phosphodiesterase and in the cytoplasm as a regulator of cell signaling. In this paper we show that in response to proteasome inhibition TTRAP accumulates in nucleolar cavities in a promyelocytic leukemia protein-dependent manner. In the nucleolus, TTRAP contributes to control levels of ribosomal RNA precursor and processing intermediates, and this phenotype is independent from its 5'-tyrosyl DNA phosphodiesterase activity. Our findings suggest a previously unidentified function for TTRAP and nucleolar cavities in ribosome biogenesis under stress.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Line, Tumor
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Cell Nucleolus / genetics
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Cell Nucleolus / metabolism*
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DNA-Binding Proteins
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HEK293 Cells
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Humans
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Phosphoric Diester Hydrolases
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Promyelocytic Leukemia Protein
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Proteasome Endopeptidase Complex / genetics
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Proteasome Endopeptidase Complex / metabolism
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Proteasome Inhibitors*
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RNA Processing, Post-Transcriptional / physiology*
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RNA, Ribosomal / genetics
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RNA, Ribosomal / metabolism*
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Ribosomes / genetics
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Ribosomes / metabolism*
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Signal Transduction / physiology*
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Stress, Physiological / physiology
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Tumor Suppressor Proteins / genetics
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Tumor Suppressor Proteins / metabolism*
Substances
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DNA-Binding Proteins
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Nuclear Proteins
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Promyelocytic Leukemia Protein
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Proteasome Inhibitors
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RNA, Ribosomal
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Transcription Factors
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Tumor Suppressor Proteins
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PML protein, human
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Phosphoric Diester Hydrolases
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TDP2 protein, human
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Proteasome Endopeptidase Complex