Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity.

By W. Zeng, Lijun Sun, Xiaomo Jiang, Xiang Chen, F. Hou, Anirban Adhikari, Ming Xu, Zhijian J. Chen. Cell, 2010

648 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/b7fe80bba567273484b54ab57ae1b7fb4b94633c

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In Immunology

Citations in the corpus

The ubiquitin code. (2012, background): “Lys63-linked chains activate IKK by promoting its binding to the upstream TAK1 that distinct types of ubiquitin topologies, i.e., Met1-, Lys11/Lys63-, Lys63-, or Lys48-linked chains, regulate signaling through inhibitor degradation, proteasomal processing, allosteric”
A minimal RNA ligand for potent RIG-I activation in living mice (2017, background): “These findings challenged the notion that RIG-I forms functional aggregates on RNA, suggesting that RIG-I/MAVS oligomerization is mediated by other features, such as ubiquitination of the CARD domains (28-30).”
MAVS Forms Functional Prion-Like Aggregates To Activate and Propagate Antiviral Innate Immune Response (2011, background): “This is consistent with our previous estimate that less than 20 molecules of viral RNA and K63 ubiquitin chains in a cell are sufficient to cause detectable IRF3 activation (Zeng et al., 2010).”
Pathogen Recognition by the Innate Immune System (2011, background): “Furthermore, free K63-linked ubiquitin chains activate RIG-I-dependent downstream signaling, suggesting that free ubiquitin chains are the endogenous ligands of RIG-I [73].”
The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain (2014, background): “During this process, the CARDs are expelled from HEL2i into solution, making them available for covalent ubiquitination by TRIM25 (32) or non-covalent binding with free K63-linked tetra-ubiquitin chains (33,34), and subsequent activation of MAVS.”
Signaling in innate immunity and inflammation. (2012, background): “In an ill-defined manner, this interaction causes RIG-I to engage the mitochondrial CARD-containing protein MAVS (also called IPS-1, VISA, and Cardif ) (Zeng et al. 2010).”
Cytosolic Sensing of Viruses (2013, background): “Lys172 of the free CARD2 is now available for the addition of polyubiquitin chains generated by the E3 ligase TRIM25 (tripartite-motif-containing 25), although it remains unclear whether those chains are bound covalently or noncovalently (Gack et al., 2007; Zeng et al., 2010).”
A structure-based model of RIG-I activation. (2012, background): “RIG-I was first reported as a retinoic acid–inducible gene in 1997 (GenBank: AF038963) and later rediscovered in the pig as a helicase (denoted RHIV-1) induced upon infection with porcine reproductive and respiratory syndrome virus (Zhang et al. 2000).”
Immune signaling by RIG-I-like receptors (2011, background): “However, free K63-linked polyubiquitin chains are capable of inducing RIG-I activation in an in vitro reconstitution of the RIG-I pathway, suggesting that it is K172mediated polyubiquitin binding and not ubiquitin modification that might drive RIG-I activation (Zeng et al., 2010).”