References
- Bai, Y., Yang, C., Hu, K., Elly, C., and Liu, Y.C. (2004). Itch E3 ligase-mediated regulation of TGF-beta signaling by modulating smad2 phosphorylation. Mol. Cell 15, 825-831. https://doi.org/10.1016/j.molcel.2004.07.021
- Derynck, R., and Akhurst, R.J. (2007). Differentiation plasticity regulated by TGF-beta family proteins in development and disease. Nat. Cell Biol. 9, 1000-1004. https://doi.org/10.1038/ncb434
- Fang, D., Elly, C., Gao, B., Fang, N., Altman, Y., Joazeiro, C., Hunter, T., Copeland, N., Jenkins, N., and Liu, Y.C. (2002). Dysregulation of T lymphocyte function in itchy mice: a role for Itch in TH2 differentiation. Nat. Immunol. 3, 281-287. https://doi.org/10.1038/ni763
- Ho, K.C., Zhou, Z., She, Y.M., Chun, A., Cyr, T.D., and Yang, X. (2011). Itch E3 ubiquitin ligase regulates large tumor suppressor 1 stability [corrected]. Proc. Natl. Acad. Sci. USA 108, 4870-4875. https://doi.org/10.1073/pnas.1101273108
- Kavsak, P., Rasmussen, R.K., Causing, C.G., Bonni, S., Zhu, H., Thomsen, G.H., and Wrana, J.L. (2000). Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol. Cell 6, 1365-1375. https://doi.org/10.1016/S1097-2765(00)00134-9
- Kwon, A., Lee, H.L., Woo, K.M., Ryoo, H.M., and Baek, J.H. (2013). SMURF1 plays a role in EGF-induced breast cancer cell migration and invasion. Mol. Cells 36, 548-555. https://doi.org/10.1007/s10059-013-0233-4
- Lallemand, F., Seo, S.R., Ferrand, N., Pessah, M., L'Hoste, S., Rawadi, G., Roman-Roman, S., Camonis, J., and Atfi, A. (2005). AIP4 restricts transforming growth factor-beta signaling through a ubiquitination-independent mechanism. J. Biol. Chem. 280, 27645-27653. https://doi.org/10.1074/jbc.M500188200
- Lohr, N.J., Molleston, J.P., Strauss, K.A., Torres-Martinez, W., Sherman, E.A., Squires, R.H., Rider, N.L., Chikwava, K.R., Cummings, O.W., Morton, D.H., et al. (2010). Human ITCH E3 ubiquitin ligase deficiency causes syndromic multisystem autoimmune disease. Am. J. Hum. Genet. 86, 447-453. https://doi.org/10.1016/j.ajhg.2010.01.028
- Perry, W.L., Hustad, C.M., Swing, D.A., O'Sullivan, T.N., Jenkins, N.A., and Copeland, N.G. (1998). The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat. Genet. 18, 143-146. https://doi.org/10.1038/ng0298-143
- Rossi, M., Aqeilan, R.I., Neale, M., Candi, E., Salomoni, P., Knight, R.A., Croce, C.M., and Melino, G. (2006). The E3 ubiquitin ligase Itch controls the protein stability of p63. Proc. Natl. Acad. Sci. USA 103, 12753-12758. https://doi.org/10.1073/pnas.0603449103
- Salah, Z., Melino, G., and Aqeilan, R.I. (2011). Negative regulation of the Hippo pathway by E3 ubiquitin ligase ITCH is sufficient to promote tumorigenicity. Cancer Res. 71, 2010-2020. https://doi.org/10.1158/0008-5472.CAN-10-3516
- Schwarz, S.E., Rosa, J.L., and Scheffner, M. (1998). Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J. Biol. Chem. 273, 12148-12154. https://doi.org/10.1074/jbc.273.20.12148
- Shi, Y., and Massague, J. (2003). Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113, 685-700. https://doi.org/10.1016/S0092-8674(03)00432-X
- Su, J., and Liu, Y.C. (2010). Foxp3 positive regulatory T cells: a functional regulation by the E3 ubiquitin ligase Itch. Semin. Immunopathol. 32, 149-156. https://doi.org/10.1007/s00281-009-0192-1
- Venuprasad, K., Huang, H., Harada, Y., Elly, C., Subramaniam, M., Spelsberg, T., Su, J., and Liu, Y.C. (2008). The E3 ubiquitin ligase Itch regulates expression of transcription factor Foxp3 and airway inflammation by enhancing the function of transcription factor TIEG1. Nat. Immunol. 9, 245-253. https://doi.org/10.1038/ni1564
- Wei, W., Li, M., Wang, J., Nie, F., and Li, L. (2012). The E3 ubiquitin ligase ITCH negatively regulates canonical Wnt signaling by targeting dishevelled protein. Mol. Cell. Biol. 32, 3903-3912. https://doi.org/10.1128/MCB.00251-12
- Woo, C.H., Shishido, T., McClain, C., Lim, J.H., Li, J.D., Yang, J., Yan, C., and Abe, J. (2008). Extracellular signal-regulated kinase 5 SUMOylation antagonizes shear stress-induced antiinflammatory response and endothelial nitric oxide synthase expression in endothelial cells. Circ. Res. 102, 538-545. https://doi.org/10.1161/CIRCRESAHA.107.156877
- Wood, J.D., Yuan, J., Margolis, R.L., Colomer, V., Duan, K., Kushi, J., Kaminsky, Z., Kleiderlein, J.J., Sharp, A.H., and Ross, C.A. (1998). Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins. Mol. Cell. Neurosci. 11, 149-160. https://doi.org/10.1006/mcne.1998.0677
- Zhang, S., Fei, T., Zhang, L., Zhang, R., Chen, F., Ning, Y., Han, Y., Feng, X.H., Meng, A., and Chen, Y.G. (2007). Smad7 antagonizes transforming growth factor beta signaling in the nucleus by interfering with functional Smad-DNA complex formation. Mol. Cell. Biol. 27, 4488-4499. https://doi.org/10.1128/MCB.01636-06
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