Publication Date:
2019
Description:
〈sec〉〈st〉Synopsis〈/st〉〈p〉〈textbox textbox-type="graphic"〉〈p〉〈inline-fig〉〈/inline-fig〉〈/p〉〈/textbox〉〈/p〉
〈p〉Viral infection triggers the formation of mitochondrial antiviral signaling protein (MAVS) aggregates, which potently promote immune signaling. However, the exact molecular mechanism underlying the targeted autophagic degradation of MAVS remains unclear. Here, we investigated the mechanism by which RNF34 regulates immunity and mitophagy by targeting MAVS.〈/p〉
〈p〉 〈l type="unord"〉〈li〉〈p〉RNF34 negatively regulates RIG-I like receptor (RLR)-mediated antiviral immunity.〈/p〉〈/li〉
〈li〉〈p〉RNF34 catalyzes the K27/K29-linked ubiquitination of MAVS at Lys 297, 311, 348, and 362.〈/p〉〈/li〉
〈li〉〈p〉RNF34 initiates the K63- to K27-linked ubiquitination transition on MAVS primarily at Lys 311.〈/p〉〈/li〉
〈li〉〈p〉RNF34 facilitates the autophagic degradation of MAVS.〈/p〉〈/li〉
〈li〉〈p〉RNF34 promotes NDP52-dependent selective mitophagy.〈/p〉〈/li〉〈/l〉 〈/p〉〈/sec〉
Print ISSN:
0261-4189
Electronic ISSN:
1460-2075
Topics:
Biology
,
Medicine
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