Abstract
Primary response transcription factor, Egr-1, is rapidly activated by a variety of extracellular stimuli. Activation of Egr-1 is shown to function as a master switch activated by ischemia to trigger expression of pivotal regulators of inflammation, coagulation and vascular hyperpermeability. Egr-1 is a short-lived protein, but the mechanism that regulates its stability has not yet been clarified. In this study, the yeast two-hybrid screening revealed that Egr-1 interacts significantly with PRC8 (proteasome component C8) and the specific interaction was confirmed by GST pull-down assay and coimmunoprecipitation. Interestingly, we found that the PRC8-mediated regulation of Egr-1 activity is associated with the proteasome pathway and PRC8 inhibits the transcriptional activity of Egr-1. In addition, Egr-1 protein was specifically multiubiquitinated by ubiquitin. These data strongly imply that Egr-1 protein is targeted for proteolysis by the ubiquitin-dependent proteasome pathway.
| Original language | English |
|---|---|
| Pages (from-to) | 163-167 |
| Number of pages | 5 |
| Journal | Biochimica et Biophysica Acta - Molecular Cell Research |
| Volume | 1592 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 21 Oct 2002 |
Bibliographical note
Funding Information:Financial support was from the National Research Laboratory Fund (2000-N-NL-01-C-015), the Ministry of Science and Technology, Korea (to K-W. K).
Keywords
- Egr-1
- Proteasome
- Protein degradation
- Ubiquitin
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