ebi regulates epidermal growth factor receptor signaling pathways in Drosophila. Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack. PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism. Seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination.
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The ubiquitin-proteasome pathway: on protein death and cell life. Therefore, Siah proteins share important similarities with the TRAF family of proteins, including their overall domain architecture, three-dimensional structure and functional activity.Ĭiechanover, A.
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We find that the Siah1a SBD potentiates TNF-α-mediated NF-κB activation. The Siah structure also reveals two novel zinc fingers in a region with sequence similarity to TRAF. The TRAF-C region interacts with TNF-α receptors and TNF-receptor associated death-domain (TRADD) proteins however, our findings indicate that these interactions are unlikely to be mimicked by Siah. The structure reveals that Siah is a dimeric protein and that the SBD adopts an eight-stranded β-sandwich fold that is highly similar to the TRAF-C region of TRAF (TNF-receptor associated factor) proteins.
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We have determined the crystal structure of the substrate-binding domain (SBD) of murine Siah1a to 2.6 Å resolution. Members of the Siah ( seven in absentia homolog) family of RING domain proteins are components of E3 ubiquitin ligase complexes that catalyze ubiquitination of proteins.