A role for ebi in neuronal cell cycle control. 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. 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. 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. 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.
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