Figure 1

Figure 1. From: Prion-like behavior of MAVS in RIG-I signaling.

Hypothetical model of the switch to the prion-like form of MAVS. (A) The switch may be triggered by interactions between the non-prion CARD domain of MAVS (blue) and the CARD domains of dimers or oligomers of RIG-I (green), which induce a conformational alteration promoting the prion-like state of MAVS (teal). Once converted to this state, activated MAVS forms aggregates, possibly in a left-handed helix formation as has been observed in the Myddosome, which also interfaces with TRAF3 and TRAF6 to transduce signaling. Model of MAVS CARD domain (Protein Data Bank Accession 2VGQ) was generated using UCSF Chimera. (B) RIG-I signaling. 5′-triphosphorylated RNA from DNA or RNA viruses binds to the C-terminal domain (RD/CTD) of RIG-I, causing it to release autoinhibitory interactions. Full activation of RIG-I requires binding to unanchored K63 polyubiquitin chains (K63), as well as conjugation to K63 polyubiquitin chains by TRIM25 and Riplet/RNF135. CARD-CARD interactions between RIG-I and MAVS lead to MAVS activation, which involves a switch to the prion-like conformation and aggregation into large polymers. These polymers activate TRAF6 and TRAF3, leading to NF-κB- and IRF3-dependent gene transcription.

Eva Marie Y Moresco, et al. Cell Res. 2011 December;21(12):1643-1645.

Supplemental Content

Filter your results:

Search details

See more...

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk