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Identification of interaction between PAI-2 and IRF-3
Yu-Qing Zhang1, Ping Li, Min Hou
1Department of Molecular Genetics, Shanghai Medical School of Fudan University; Key Laboratory of Molecular Medicine, Ministry of Education, Shanghai 200032, China.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|July 29, 2003
Summary
Plasminogen activator inhibitor-2 (PAI-2) protects cells from tumor necrosis factor-alpha-induced apoptosis. This study identifies interferon regulatory factor-3 (IRF-3) as a key interacting protein involved in PAI-2
Area of Science:
- Cell biology
- Molecular biology
- Immunology
Background:
- Plasminogen activator inhibitor-2 (PAI-2) confers protection against tumor necrosis factor-alpha (TNF-α)-induced apoptosis.
- A specific 33-amino acid fragment within PAI-2 (between helix C and D) is crucial for this protective effect, suggesting interaction with intracellular proteins.
Purpose of the Study:
- To identify intracellular proteins that interact with the apoptosis-protective fragment of PAI-2.
- To elucidate the molecular mechanisms underlying PAI-2-mediated apoptosis protection.
Main Methods:
- Yeast two-hybrid system screening of a HeLa cell cDNA library using the PAI-2 helical fragment as bait.
- Co-immunoprecipitation assays to confirm in vivo interaction between PAI-2 and identified proteins.
Main Results:
- A 98-amino acid C-terminal fragment of interferon regulatory factor-3 (IRF-3) was identified as an interacting partner of the PAI-2 fragment.
- Co-immunoprecipitation confirmed the in vivo interaction between PAI-2 and IRF-3.
Conclusions:
- Interferon regulatory factor-3 (IRF-3) interacts with PAI-2.
- IRF-3 may play a role in the apoptosis-protective and antiviral functions of PAI-2.