We are analyzing https://link.springer.com/article/10.1186/1750-2187-8-7.

Title:
TRAF molecules in cell signaling and in human diseases | Journal of Molecular Signaling
Description:
The tumor necrosis factor receptor (TNF-R)-associated factor (TRAF) family of intracellular proteins were originally identified as signaling adaptors that bind directly to the cytoplasmic regions of receptors of the TNF-R superfamily. The past decade has witnessed rapid expansion of receptor families identified to employ TRAFs for signaling. These include Toll-like receptors (TLRs), NOD-like receptors (NLRs), RIG-I-like receptors (RLRs), T cell receptor, IL-1 receptor family, IL-17 receptors, IFN receptors and TGFβ receptors. In addition to their role as adaptor proteins, most TRAFs also act as E3 ubiquitin ligases to activate downstream signaling events. TRAF-dependent signaling pathways typically lead to the activation of nuclear factor-κBs (NF-κBs), mitogen-activated protein kinases (MAPKs), or interferon-regulatory factors (IRFs). Compelling evidence obtained from germ-line and cell-specific TRAF-deficient mice demonstrates that each TRAF plays indispensable and non-redundant physiological roles, regulating innate and adaptive immunity, embryonic development, tissue homeostasis, stress response, and bone metabolism. Notably, mounting evidence implicates TRAFs in the pathogenesis of human diseases such as cancers and autoimmune diseases, which has sparked new appreciation and interest in TRAF research. This review presents an overview of the current knowledge of TRAFs, with an emphasis on recent findings concerning TRAF molecules in signaling and in human diseases.
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Keywords {🔍}

traf, google, scholar, pubmed, article, cas, signaling, activation, cell, trafs, receptor, cells, factor, receptors, nfκb, biol, protein, immunol, mice, nfkappab, proteins, tlr, response, type, irf, immune, klinked, complex, wang, tumor, family, immunity, ubiquitination, chem, production, tolllike, domain, pathways, human, regulates, phosphorylation, nod, necrosis, responses, diseases, pathway, ciap, expression, including, mol,

Topics {✒️}

interleukin-1beta-induced ikk/nf-kappab c-raf-mek-erk-dependent phosphorylation c-jun n-terminal kinase ripk1/rip1-mediated mapk8/jnk activation carma1-malt1-bcl10-pkcθ-ikk-caspase 8 virus-induced nf-kappab activation inhibit tlr-mediated nf-kappab ubiquitin-mediated nf-kappab activation gitr-induced nf-kappab activation nf-kappab-inducing kinase il-17-induced nf-kappab activation regulate tnf-induced nf-kappab traf6-mediated k63-linked polyubiquitination receptor-mediated nf-kappab activation ciap1/2-catalyzed k48-linked polyubiquitination ciap1/2-catalyzed k63-linked ubiquitination nod-induced nf-kappab activation v-flip member mc159 act1-mediated k63-linked ubiquitination tnf-r2-induced jnk activation ifn-induced nf-κb2 activation traf5-mediated nf-kappab activation negatively regulates nf-κb nod-induced nf-κb activation tlr-driven nf-κb activation xedar-mediated nf-κb activation n-terminal coiled-coil region k63-linked polyubiquitin chains traf6-nf-kappab signaling pathways c-terminal transmembrane domain c-terminal β-sandwich c-iap1 mediate ubiquitination il-17-induced act1-traf2-traf5 interaction k63-linked auto-ubiquitination rig-i-mavs-traf6 signaling leads noncanonical nf-kappab pathway receptor kinase-independent manner tgf-beta-mediated suppression mitogen-activated protein kinases il-17r-act1-traf2-traf5 complex noncanonical nf-kappab signaling alternative nf-kappab pathways conventional k63-linked polyubiquitination t-cell intrinsic effects alternative nf-kappab pathway oxidized ldl-induced apoptosis tnfsf10/trail-induced apoptosis degradative k63-linked polyubiquitination full-length trafs/substrates remains factor-dependent nf-kappa

Questions {❓}

(1) What is the stoichiometric composition of TRAFs and other signaling proteins in each signaling complex?
(2) How is the E3 ligase activity of each TRAF regulated precisely?
(3) What are the molecular structures of each TRAF in complex with its specific signaling partner, substrate, or enzyme?
(4) Are there additional pathogenic factors of invading microorganisms that target TRAFs during infections?
(6) What are the cell type-specific factors that dictate cell type-specific TRAF functions?
(7) Are there additional TRAF genetic alterations and SNPs associated with human diseases?
Bonardi V, Cherkis K, Nishimura MT, Dangl JL: A new eye on NLR proteins: focused on clarity or diffused by complexity?
How does each TRAF act in such complex and concerted signaling pathways in different cellular context during infection?

Schema {🗺️}

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      headline:TRAF molecules in cell signaling and in human diseases
      description:The tumor necrosis factor receptor (TNF-R)-associated factor (TRAF) family of intracellular proteins were originally identified as signaling adaptors that bind directly to the cytoplasmic regions of receptors of the TNF-R superfamily. The past decade has witnessed rapid expansion of receptor families identified to employ TRAFs for signaling. These include Toll-like receptors (TLRs), NOD-like receptors (NLRs), RIG-I-like receptors (RLRs), T cell receptor, IL-1 receptor family, IL-17 receptors, IFN receptors and TGFβ receptors. In addition to their role as adaptor proteins, most TRAFs also act as E3 ubiquitin ligases to activate downstream signaling events. TRAF-dependent signaling pathways typically lead to the activation of nuclear factor-κBs (NF-κBs), mitogen-activated protein kinases (MAPKs), or interferon-regulatory factors (IRFs). Compelling evidence obtained from germ-line and cell-specific TRAF-deficient mice demonstrates that each TRAF plays indispensable and non-redundant physiological roles, regulating innate and adaptive immunity, embryonic development, tissue homeostasis, stress response, and bone metabolism. Notably, mounting evidence implicates TRAFs in the pathogenesis of human diseases such as cancers and autoimmune diseases, which has sparked new appreciation and interest in TRAF research. This review presents an overview of the current knowledge of TRAFs, with an emphasis on recent findings concerning TRAF molecules in signaling and in human diseases.
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         Protein-Ligand Interactions
         Cell Biology
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