![]() ![]() Nature Cell Biology, 10, 812–824.īuchwald, M., Pietschmann, K., Brand, P., Gunther, A., Mahajan, NP., Heinze,l T., and Kramer OH (2012) SIAH ubiquitin ligases target the nonreceptor tyrosine kinase ACK1 for ubiquitinylation and proteasomal degradation. Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR. ![]() Winter, M., Sombroek, D., Dauth, I., Moehlenbrink, J., Scheuermann, K., Crone, J., et al. An inducible autoregulatory loop between HIPK2 and Siah2 at the apex of the hypoxic response. A., de la Vega, L., Moller, A., Bowtell, D. Biochemical and Biophysical Research Communications, 397, 391–396.Ĭalzado, M. SIAH-1 interacts with mammalian polyhomeotic homologues HPH2 and affects its stability via the ubiquitin-proteasome pathway. Wu, H., Lin, Y., Shi, Y., Qian, W., Tian, Z., Yu, Y., et al. Biochemical and Biophysical Research Communications, 399, 623–628. The Ski protein negatively regulates Siah2-mediated HDAC3 degradation. ![]() The ubiquitin ligase Siah2 regulates PPARgamma activity in adipocytes. SIAH-mediated ubiquitination and degradation of acetyl-transferases regulate the p53 response and protein acetylation. Grishina, I., Debus, K., Garcia-Limones, C., Schneider, C., Shresta, A., Garcia, C., et al. The ubiquitin ligase Siah1 controls ELL2 stability and formation of super elongation complexes to modulate gene transcription. Molecular and Cellular Biology, 23, 9150–9161. Generation and analysis of Siah2 mutant mice. Molecular and Cellular Biology, 22, 6854–6865.įrew, I. Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to the substrate protein tramtrack. Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. Isolation and characterisation of murine homologues of the Drosophila seven in absentia gene (sina). ![]() PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism. Regulation of human placental development by oxygen tension. Degrading liaisons: Siah structure revealed. Non-traditional functions of ubiquitin and ubiquitin-binding proteins. Annual Review of Biochemistry, 67, 425–479. ![]()
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