Abstract
The NLR (nucleotide-binding domain leucine-rich repeat containing) proteins serve as regulators of inflammatory signaling pathways. NLRX1, a mitochondria-localized NLR protein, has been previously shown to negatively regulate inflammatory cytokine production activated via the MAVSDDX58 (RIG-I) pathway. The literature also indicates that DDX58 has a negative impact upon autophagy. Consistent with the inhibitory role of NLRX1 on DDX58, our recent study indicates a role of NLRX1 in augmenting virus-induced autophagy. This effect is through its interaction with another mitochondrial protein TUFM (Tu translation elongation factor, mitochondrial, also known as EF-TuMT, COXPD4, and P43). TUFM also reduces DDX58-activated cytokines but augments autophagy. Additionally it interacts with ATG12-ATG5-ATG16L1 to form a molecular complex that modulates autophagy. The work shows that both NLRX1 and TUFM work in concert to reduce cytokine response and augment autophagy.
Original language | English (US) |
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Pages (from-to) | 432-433 |
Number of pages | 2 |
Journal | Autophagy |
Volume | 9 |
Issue number | 3 |
DOIs | |
State | Published - Mar 2013 |
Externally published | Yes |
Keywords
- Atg12
- Atg16L1
- Atg5
- Autophagy
- Interferon
- NLRX1
- RIG-I
- RLR
- TUFM
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology