MLL5 suppresses antiviral innate immune response by facilitating STUB1-mediated RIG-I degradation

• Main Authors: Zhou, P, Ding, X, Wan, X, Liu, L, Yuan, X, Zhang, W, Hui, X, Meng, G, Xiao, H, Li, B, Zhong, J, Hou, F, Deng, L, Zhang, Y
• Other Authors: BIOCHEMISTRY
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: protein; protein MLL5; protein STUB1; retinoic acid inducible protein I; ubiquitin protein ligase E3; unclassified drug; antivirus agent; Ddx58 protein, mouse; DNA binding protein; histone lysine methyltransferase; MLL5 protein, human; MLL5 protein, mouse; proteasome; STUB1 protein, human; Stub1 protein, mouse; ubiquitin protein ligase; cytoplasm; degradation; gene; gene expression; genetic analysis; immune response; rodent; animal cell; animal experiment; animal model; animal tissue; antiviral activity; Article; controlled study; embryo; female; human; human cell; in vitro study; in vivo study; innate immunity; mouse; nonhuman; protein function; Sendai virus; ubiquitination; Vesiculovirus; virus infection; virus load; virus replication; animal; C57BL mouse; CRISPR Cas system; DNA damage; HEK293 cell line; immunology; male; metabolism; rhabdovirus infection; RNA interference; signal transduction; Vesicular stomatitis Indiana virus; Mus; Vesicular stomatitis virus; Animals; Antiviral Agents; CRISPR-Cas Systems; Cytoplasm; DEAD Box Protein 58; DNA Damage; DNA-Binding Proteins; Female; HEK293 Cells; Histone-Lysine N-Methyltransferase; Humans; Immunity, Innate; Male; Mice; Mice, Inbred C57BL; Proteasome Endopeptidase Complex; Rhabdoviridae Infections; RNA Interference; Signal Transduction; Ubiquitin-Protein Ligases; Ubiquitination; Virus Replication
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/178419
• Institution: National University of Singapore

10.1038/s41467-018-03563-8