ARF-like Protein 16 (ARL16) Inhibits RIG-I by Binding with Its C-terminal Domain in a GTP-dependent Manner

• DOI: 10.1074/jbc.m110.206896
• Publication Date: 2011-01-14T05:06:17Z
• Authors: Yong-Kang Yang; Hong Qu; Dong Gao; Wei Di; Hai-Wei Chen; Xin Guo; Zhong-He Zhai; Dan-Ying Chen
• Keywords: C-terminus; GTP-binding protein regulators

Retinoic acid-inducible gene I (RIG-I) recognizes RNA virus-derived nucleic acids, which leads to the production of type interferon (IFN) in most cell types. Tight regulation RIG-I activity is important prevent ultra-immune responses. In this study, we identified an ARF-like (ARL) family member, ARL16, as a protein that interacts with RIG-I. Overexpression but not its homologous proteins ARL1 and ARF1, inhibited RIG-I-mediated downstream signaling antiviral activity. Knockdown endogenous ARL16 by RNAi potentiated Sendai virus-induced IFN-β expression vesicular stomatitis virus replication. interacted C-terminal domain (CTD) suppress association between RNA. (T37N) ARL16Δ45-54, were restricted GTP-disassociated form, did interact also lost inhibitory function. Furthermore, suggest changes GTP binding status upon viral infection binds CTD negatively control These findings suggested novel innate immune function for ARL GTP-dependent model regulated.