Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions.

The Journal of Biological Chemistry
Amitava MukherjeeCarolyn B Coyne

Abstract

The actin cytoskeleton serves as a barrier that protects mammalian cells from environmental pathogens such as bacteria, fungi, and viruses. Several components of antimicrobial signaling pathways have been shown to associate directly with the actin cytoskeleton, indicating that the cytoskeleton may also serve as a platform for immune-associated molecules. Here we report that retinoic acid-induced gene-I (RIG-I), an important viral RNA recognition molecule, is associated with the actin cytoskeleton and localizes predominantly to actin-enriched membrane ruffles in non-polarized epithelial cells. Subcellular localization and fractionation experiments revealed that the association between RIG-I and the actin cytoskeleton was mediated by its N-terminal caspase activation and recruitment domains (CARDs), which were necessary and sufficient to induce cytoskeletal association. We also show that RIG-I plays a role in cellular migration, as ectopic expression of RIG-I enhanced cellular migration in a wound healing assay and depletion of endogenous RIG-I significantly reduced wound healing. We further show that in both cultured intestinal epithelial cells (IEC) and human colon and small intestine biopsies, RIG-I is enriched at apico-latera...Continue Reading

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Citations

Jan 12, 2013·Antioxidants & Redox Signaling·Fiorella BiasiGiuseppe Poli
Jan 15, 2011·Clinical Microbiology Reviews·Marjolaine VareilleNicolas Regamey
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Jan 24, 2021·Seminars in Cancer Biology·Mohammad Imran KhanHasan Mukhtar
Jun 30, 2019·Current Medicinal Chemistry·Daniel H O' DonovanDeanna A Mele

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