| Autor: |
Teague, Helena C., Lefevre, Charlotte, Rieser, Eva, Wolfram, Lina, de Miguel, Diego, Patricio de Oliveira, Daniel, Oliveira, Marisa, Mansur, Daniel S., Irigoyen, Nerea, Walczak, Henning, Ferguson, Brian J. |
| Zdroj: |
Cell Death and Differentiation; January 2024, Vol. 31 Issue: 1 p28-39, 12p |
| Abstrakt: |
The ability of cells to mount an interferon response to virus infections depends on intracellular nucleic acid sensing pattern recognition receptors (PRRs). RIG-I is an intracellular PRR that binds short double-stranded viral RNAs to trigger MAVS-dependent signalling. The RIG-I/MAVS signalling complex requires the coordinated activity of multiple kinases and E3 ubiquitin ligases to activate the transcription factors that drive type I and type III interferon production from infected cells. The linear ubiquitin chain assembly complex (LUBAC) regulates the activity of multiple receptor signalling pathways in both ligase-dependent and -independent ways. Here, we show that the three proteins that constitute LUBAC have separate functions in regulating RIG-I signalling. Both HOIP, the E3 ligase capable of generating M1-ubiquitin chains, and LUBAC accessory protein HOIL-1 are required for viral RNA sensing by RIG-I. The third LUBAC component, SHARPIN, is not required for RIG-I signalling. These data cement the role of LUBAC as a positive regulator of RIG-I signalling and as an important component of antiviral innate immune responses. |
| Databáze: |
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