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Tetherin Suppresses Type I Interferon Signaling by Targeting MAVS for NDP52-Mediated Selective Autophagic Degradation in Human Cells.

Molecular cell | Oct 19, 2017

Tetherin (BST2/CD317) is an interferon-inducible antiviral factor known for its ability to block the release of enveloped viruses from infected cells. Yet its role in type I interferon (IFN) signaling remains poorly defined. Here, we demonstrate that Tetherin is a negative regulator of RIG-I like receptor (RLR)-mediated type I IFN signaling by targeting MAVS. The induction of Tetherin by type I IFN accelerates MAVS degradation via ubiquitin-dependent selective autophagy in human cells. Moreover, Tetherin recruits E3 ubiquitin ligase MARCH8 to catalyze K27-linked ubiquitin chains on MAVS at lysine 7, which serves as a recognition signal for NDP52-dependent autophagic degradation. Taken together, our findings reveal a negative feedback loop of RLR signaling generated by Tetherin-MARCH8-MAVS-NDP52 axis and provide insights into a better understanding of the crosstalk between selective autophagy and optimal deactivation of type I IFN signaling.

Pubmed ID: 28965816 RIS Download

Mesh terms: A549 Cells | Adaptor Proteins, Signal Transducing | Animals | Antigens, CD | Autophagy | DEAD Box Protein 58 | GPI-Linked Proteins | HeLa Cells | Humans | Interferon Type I | Mice | Nuclear Proteins | RAW 264.7 Cells | Signal Transduction | Ubiquitin | Ubiquitin-Protein Ligases | Ubiquitination

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