Journal
MOLECULAR CELL
Volume 55, Issue 4, Pages 511-523Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2014.06.010
Keywords
-
Categories
Funding
- CIHR [MOP 125865] Funding Source: Medline
- Howard Hughes Medical Institute Funding Source: Medline
- NCI NIH HHS [P30 CA044579] Funding Source: Medline
- NIAID NIH HHS [R01 AI106912] Funding Source: Medline
- NIBIB NIH HHS [EB001567, R01 EB001567] Funding Source: Medline
- NIGMS NIH HHS [GM R01 60635, R01 GM060635, GM U54 094598, U54 GM094598] Funding Source: Medline
Ask authors/readers for more resources
RIG-I activates interferon signaling pathways by promoting filament formation of the adaptor molecule, MAVS. Assembly of the MAVS filament is mediated by its CARD domain (CARD(MAVS)), and requires its interaction with the tandem CARDs of RIG-I (2CARD(RIG-I)). However, the precise nature of the interaction between 2CARD(RIG-I) and CARD(MAVS), and how this interaction leads to CARD(MAVS) filament assembly, has been unclear. Here we report a 3.6 angstrom electron microscopy structure of the CARD(MAVS) filament and a 3.4 angstrom crystal structure of the 2CARD(RIG-I):CARD(MAVS) complex, representing 2CARD(RIG-I) caught in the act of nucleating the CARD MAVS filament. These structures, together with functional analyses, show that 2CARD(RIG-I) acts as a template for the CARD(MAVS) filament assembly, by forming a helical tetrameric structure and recruiting CARD(MAVS) along its helical trajectory. Our work thus reveals that signal activation by RIG-I occurs by imprinting its helical assembly architecture on MAVS, a previously uncharacterized mechanism of signal transmission.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available