TRAF6/or TRAF2 ubiquitination within dsRNA:Mda5:Ips1:Traf6/ or Traf2 complex

Stable Identifier
R-GGA-1227769
Type
Reaction [omitted]
Species
Gallus gallus
Related Species
Infectious bronchitis virus
Compartment
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TRAFs are E3 ubiquitin ligases that bind to an E2 - ubiquitin thioester and catalyse Lys63-ubquitination on the associated target proteins and possibly on themselves [Lamothe B et al 2007, Mao AP et al 201]. Although TRAF2 failed to interact with a number of E2 ligases related to Ubc13 and showed considerable difference in its RING domain structure from the known TRAF6 RING structure [Yin Q et al 2009], yet TRAF2 is believed to act as an E3 ubiquitin ligase. Sphingosine-1-phosphate (S1P), which is synthesized during inflammatory responces, was shown to bind to TRAF2 and stimulate TRAF2-mediated K63-linked polyubiquitination [Alvarez SE et al 2010; Napolitano G and Karin M 2010]

Literature References
PubMed ID Title Journal Year
11057907 Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain

Deng, L, Wang, C, Spencer, E, Yang, L, Braun, A, You, J, Slaughter, C, Pickart, C, Chen, ZJ

Cell 2000
17135271 Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation

Lamothe, B, Besse, A, Campos, AD, Webster, WK, Wu, H, Darnay, BG

J Biol Chem 2007
20097753 Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response

Mao, AP, Li, S, Zhong, B, Li, Y, Yan, J, Li, Q, Teng, C, Shu, HB

J Biol Chem 2010
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
ubiquitin-ubiquitin ligase activity of dsRNA:MDA5:IPS1:TRAF6/TRAF2 [mitochondrial outer membrane]
Physical Entity
Activity
Inferred From
Authored
Reviewed
Created