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Details on Person After clustering or dimerisation lymphotoxin-beta receptor (...
| Class:Id | Summation:5676256 |
|---|---|
| _displayName | After clustering or dimerisation lymphotoxin-beta receptor (... |
| _timestamp | 2015-05-12 15:37:30 |
| created | [InstanceEdit:5676482] Garapati, Phani Vijay, 2015-02-19 |
| literatureReference | [LiteratureReference:5668539] Non-canonical NF-kB signaling pathway [LiteratureReference:5676410] Allosteric regulation of the ubiquitin:NIK and ubiquitin:TRAF3 E3 ligases by the lymphotoxin-beta receptor [LiteratureReference:5676419] Lymphotoxin-beta receptor signaling complex: role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB [LiteratureReference:5676318] TRAF5, an activator of NF-kappaB and putative signal transducer for the lymphotoxin-beta receptor |
| modified | [InstanceEdit:5692500] Garapati, Phani Vijay, 2015-05-12 |
| text | After clustering or dimerisation lymphotoxin-beta receptor (LTBR) initiates signal transduction by recruiting different TNF receptor-associated factor (TRAF) adaptors to the cytoplasmic domain. LTBR directly binds to several TRAFs, including TRAF2 and TRAF3 through its TRAF-interacting peptide motif (VanArsdale et al. 1997, Nakano et al. 1996, Sanjo et al. 2010). Mitogen-activated protein kinase kinase kinase 14 (MAP3K14 also named as NIK) is a central signalling component of the non-canonical pathway and a tight control of NIK activation by TRAFs is essential to achieve controlled activation of the noncanonical NF-kB signalling. In unstimulated cells ubiquitin:NIK E3 ligase complex catalyses K48-linked ubiquitination of NIK, leading to constitutive NIK degradation. The ubiquitin:NIK E3 ligase is a multisubunit complex comprised of TRAF3 and TRAF2 in association with cellular inhibitors of apoptosis (cIAP1,2). In the activated state the TRAF2:cIAP1,2:TRAF3:NIK complex is recruited to the receptor upon ligand binding whereupon TRAF2-mediated, K63-linked ubiquitination of cIAP1,2 switches its K48 ubiquitin ligase activity from NIK to TRAF3. The resultant TRAF3 degradation destabilizes the TRAF-cIAP complex, so allowing the accumulation of newly synthesised NIK (Razani et al. 2011, Sun 2011). |
| (summation) | [Reaction:5676593] TRAF2:TRAF1:cIAP1,2:TRAF3:NIK regulatory complex binds LTBR [Homo sapiens] |
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No pathways have been reviewed or authored by After clustering or dimerisation lymphotoxin-beta receptor (... (5676256)
