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.
Original language | English |
---|---|
Pages (from-to) | 843-855 |
Number of pages | 13 |
Journal | Molecular Cell |
Volume | 10 |
Issue number | 4 |
DOIs | |
State | Published - 1 Oct 2002 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology