Abstract
During a screen to identify c-Jun activators, we isolated a cysteine protease, SuPr-1, that induced c-Jun-dependent transcription independently of c-Jun phosphorylation. SuPr-1 is a member of a new family of proteases that hydrolyze the ubiquitin-like modifier, SUMO-1. SuPr-1 hydrolyzed SUMO-1-modified forms of the promyelocytic leukemia gene product, PML, and altered the subcellular distribution of PML in nuclear PODs (PML oncogenic domains). SuPr-1 also altered the distribution of other nuclear POD-associated proteins, such as CBP and Daxx, that act as transcriptional regulators. SuPr-1 action on transcription was enhanced by PML, and SuPr-1 failed to activate transcription in PML-deficient fibroblasts. Our studies establish an important role for SUMO proteases in transcription.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Line
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Cell Nucleus Structures / metabolism
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / metabolism*
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HeLa Cells
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Humans
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Mice
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Molecular Sequence Data
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Mutation
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Neoplasm Proteins / genetics
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Neoplasm Proteins / metabolism*
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Nuclear Proteins*
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Phosphorylation
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Promoter Regions, Genetic
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Promyelocytic Leukemia Protein
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Protein Binding
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Proto-Oncogene Proteins c-jun / metabolism
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Sequence Homology, Nucleic Acid
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Substrate Specificity
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcriptional Activation*
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Tumor Suppressor Proteins
Substances
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Neoplasm Proteins
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Nuclear Proteins
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Pml protein, mouse
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Promyelocytic Leukemia Protein
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Proto-Oncogene Proteins c-jun
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Transcription Factors
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Tumor Suppressor Proteins
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PML protein, human
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Cysteine Endopeptidases
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SENP2 protein, human
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SENP6 protein, human