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The TRAF6 RING finger domain mediates physical interaction with Ubc13
Jill Wooff1, Landon Pastushok, Michelle Hanna
1Department of Microbiology and Immunology, University of Saskatchewan, Saskatoon, SK, Canada S7N 5E5.
FEBS Letters
|May 19, 2004
Summary
Tumor necrosis factor receptor associated factor 6 (TRAF6) directly binds to the Ubc13-Uev complex, confirming its role in ubiquitination. This interaction is crucial for TRAF6
Area of Science:
- Molecular Biology
- Cell Signaling
- Protein Interactions
Background:
- Tumor necrosis factor receptor associated factor 6 (TRAF6) is a key signaling protein.
- TRAF6 functions as a ubiquitin ligase (E3) for Lys-63 polyubiquitination.
- The interaction between TRAF6 and the Ubc13-Uev (E2) complex was previously uncharacterized.
Purpose of the Study:
- To investigate the physical interaction between TRAF6 and the Ubc13-Uev E2 complex.
- To identify the domains involved in the TRAF6-Ubc13 interaction.
- To map the self-interaction domain of TRAF6.
Main Methods:
- Yeast two-hybrid assay was employed to detect protein-protein interactions.
- Site-directed mutagenesis was used to probe the interaction interface.
- Mapping of self-interaction domains was performed.
Main Results:
- TRAF6 directly interacts with the Ubc13-Uev complex via binding to Ubc13.
- Specific mutations in the TRAF6 RING finger domain or Ubc13 surface abolish this interaction.
- TRAF6 self-interaction was identified and mapped to its N-terminal RING finger motif.
Conclusions:
- Direct physical interaction between TRAF6 and Ubc13-Uev complex is confirmed.
- The study provides insights into the molecular interface for Ubc13-TRAF6 RING finger complex formation.
- Understanding this interaction is vital for elucidating TRAF6-mediated signaling pathways.