SUMO-1 protease-1 regulates gene transcription through PML Journal Article
| Authors: | Best, J. L.; Ganiatsas, S.; Agarwal, S.; Changou, A.; Salomoni, P.; Shirihai, O.; Meluh, P. B.; Pandolfi, P. P.; Zon, L. I. |
| Article Title: | SUMO-1 protease-1 regulates gene transcription through PML |
| 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. |
| Keywords: | controlled study; unclassified drug; human cell; mutation; animals; mice; gene; neoplasm proteins; cell line; protein; protein binding; genetic transcription; hela cells; phosphorylation; transcription factors; nuclear proteins; transcription regulation; amino acid sequence; molecular sequence data; tumor suppressor proteins; substrate specificity; promyelocytic leukemia; fibroblast; base sequence; sequence homology, nucleic acid; sumo 1 protein; daxx protein; cysteine endopeptidases; promoter regions (genetics); trans-activation (genetics); protein cbp; cell nucleus structures; proto-oncogene proteins c-jun; humans; human; article; brinase; supr 1 gene |
| Journal Title: | Molecular Cell |
| Volume: | 10 |
| Issue: | 4 |
| ISSN: | 1097-2765 |
| Publisher: | Cell Press |
| Date Published: | 2002-10-01 |
| Start Page: | 843 |
| End Page: | 855 |
| Language: | English |
| DOI: | 10.1016/s1097-2765(02)00699-8 |
| PUBMED: | 12419228 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
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