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Background
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SMURF2 is an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. This protein interacts with SMAD1, SMAD2 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. It enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.
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Background
References
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- Tajima, Y., et al., J. Biol. Chem. 278(12):10716-10721 (2003).
- Suzuki, C., et al., J. Biol. Chem. 277(42):39919-39925 (2002).
- Ebisawa, T., et al., J. Biol. Chem. 276(16):12477-12480 (2001).
- Zhu, H., et al., Nature 400(6745):687-693 (1999).
- Lambris, J., et al., J. Immunol. Methods 27(1):55-59 (1979).
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