Distinct molecular mechanism for initiating TRAF6 signalling

By H. Ye, J. Arron, B. Lamothe, M. Cirilli, Takashi Kobayashi, N. Shevde, D. Segal, O. Dzivenu, M. Vologodskaia, M. Yim and 6 more. Nature, 2002

716 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology

View Paper: https://www.semanticscholar.org/paper/c5161fff299a282d151d97d7278fc9cbd3e707a5

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

1. Shizuo Akira
2. Taro Kawai
3. S. Ghosh
4. M. Hayden
5. K. Takeda
6. Shintaro Sato
7. Masahiro Yamamoto
8. S. Teitelbaum

In Immunology

1. Shizuo Akira
2. Taro Kawai
3. S. Ghosh
4. M. Hayden
5. K. Takeda
6. R. Medzhitov
7. Masahiro Yamamoto
8. Shintaro Sato

Citations in the corpus

• Sequestosome 1/p62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation (2004, background): “p62 possesses a TRAF6-binding motif (60), and recent studies have shown that peptides homologous to this motif may competitively inhibit TRAF6 signaling or function (61).”
• Toll/IL-1 Receptor Domain-Containing Adaptor Inducing IFN-β (TRIF) Associates with TNF Receptor-Associated Factor 6 and TANK-Binding Kinase 1, and Activates Two Distinct Transcription Factors, NF-κB and IFN-Regulatory Factor-3, in the Toll-Like Receptor Signaling 1 (2003, background): “For example, IRAK-1, which is known to associate with the TRAF domain of TRAF6, has three TRAF6-binding motifs, and the NF- B-dependent reporter activation induced by IRAK-1 was severely reduced by the substitution of P0-residues (from glutamic acid to alanine) (12).”
• Current Understanding of RANK Signaling in Osteoclast Differentiation and Maturation (2017, background): “RANKL binding to RANK induces the trimerization of RANK and the recruitment of an adaptor protein, TRAF6, via three TRAF6-binding sites in its C-terminal cytoplasmic tail (Wong et al., 1998; Ye et al., 2002), thereby initiating the downstream signaling cascade (Fig.”
• Piriformospora indica, a cultivable root endophyte with multiple biotechnological applications (2009, background): “Three-dimensional crystal structures are known from several MATH domain proteins with bound peptide ligands (McWhirter et al., 1999; Park et al., 1999; Li et al., 2002; Ye et al., 2002).”
• Osteoclast differentiation and activation (2003, background): “TRAF6 binding to RANK has been modelled, and involves a new structure–function relationship between TRAFs and TNFR-related protein”
• Identification and Characterization of MAVS, a Mitochondrial Antiviral Signaling Protein that Activates NF-κB and IRF3 (2005, neutral): “We have examined the potential interaction of these proteins with MAVS and found that only TRAF6 could weakly associate with MAVS (Figure S5A), presumably through a putative TRAF6 binding sequence in the proline-rich region of MAVS (PGENSE, residues 153–158; Ye et al., 2002).”
• mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6 (2013, methodology): “(d) HEK293 cells were co-transfected with vectors encoding AMBRA1 together with ULK1–Myc FL (full length) or its deletion mutants encoding the kinase and the proline-rich domains (1829–1,051), and the ULK1 carboxy-terminal domain (11-828).”
• NF-κB, the first quarter-century: remarkable progress and outstanding questions. (2012, background): “TRAF6 is necessary for MyD88-dependent activation of NF-kB (Cao et al. 1996; Wesche et al. 1997; Ye et al. 2002), and TRAF6-deficient cells fail to activate NF-kB in response to IL-1 and LPS (Lomaga et al.”
• Toll-like receptor signalling (2004, background): “The consensus sequence for the TRAF6-binding domain has been identified as P-X-E-X-X-(D/E/F/W/Y”
• Genetic regulation of osteoclast development and function (2003, background): “Although this problem has not yet been resolved, the fact that, based on the crystal structure of the RANK sequence recognizing TRAF6, a cell-permeable peptide arrests osteoclastogenesis in vitro”