Distinct domains for nuclear factor-κB activation and association with tumor necrosis factor signaling proteins. I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction. A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Crystallographic analysis of CD40 recognition and signaling by human TRAF2. Structural basis for self-association and receptor recognition of human TRAF2. Park, Y.C., Burkitt, V., Villa, A.R., Tong, L. A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains. Tumor necrosis factor receptor-associated factor (TRAF) family: adapter proteins that mediate cytokine signaling. Molecular basis for CD40 signaling mediated by TRAF3. Protein structure comparison by alignment of distance matrices.
Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein–protein interactions. Insights into sequence-specific protein–DNA recognition. Structures of zinc finger domains from transcription factor Sp1. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. Ubiquitin enters the new millenium meeting review. Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis. hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways. Siah-1 mediates a novel β-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein. Siah-1, SIP, and Ebi collaborate in a novel pathway for β-catenin degradation linked to p53 responses. SIAH-1 interacts with α-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis. Proteasomal regulation of nuclear receptor corepressor-mediated repression. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mammalian homologs of seven in absentia regulate DCC via the ubiquitin- proteasome pathway. p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1. Matsuzawa, S., Takayama, S., Froesch, B.A., Zapata, J.M. 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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