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    Dhx58 DExH-box helicase 58 [ Mus musculus (house mouse) ]

    Gene ID: 80861, updated on 18-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Interferon-alpha stimulates DExH-box helicase 58 to prevent hepatocyte ferroptosis.

    Interferon-α stimulates DExH-box helicase 58 to prevent hepatocyte ferroptosis.
    Jia KW, Yao RQ, Fan YW, Zhang DJ, Zhou Y, Wang MJ, Zhang LY, Dong Y, Li ZX, Wang SY, Wang M, Li YH, Zhang LX, Lei T, Gui LC, Lu S, Yang YY, Wang SX, Yu YZ, Yao YM, Hou J., Free PMC Article

    04/22/2024
    RIG-I-Like Receptor LGP2 Is Required for Tumor Control by Radiotherapy.

    RIG-I-Like Receptor LGP2 Is Required for Tumor Control by Radiotherapy.
    Zheng W, Ranoa DRE, Huang X, Hou Y, Yang K, Poli EC, Beckett MA, Fu YX, Weichselbaum RR.

    04/13/2021
    RNA Helicase LGP2 Negatively Regulates RIG-I Signaling by Preventing TRIM25-Mediated Caspase Activation and Recruitment Domain Ubiquitination.

    RNA Helicase LGP2 Negatively Regulates RIG-I Signaling by Preventing TRIM25-Mediated Caspase Activation and Recruitment Domain Ubiquitination.
    Quicke KM, Kim KY, Horvath CM, Suthar MS., Free PMC Article

    08/15/2020
    DHX58 expression positively correlate with osteogenic process. DHX58 overexpression enhances osteogenesis via the Wnt/beta-Catenin pathway.

    DExH-Box helicase 58 enhances osteoblast differentiation of osteoblastic cells via Wnt/β-Catenin signaling.
    Zhou L, Sun S, Xu L, Yu Y, Zhang T, Wang M.

    12/28/2019
    These findings provide a unique mechanism for LGP2 negative regulation through TRAF suppression and extend the potential impact of LGP2 negative regulation beyond the IFN antiviral response.

    RNA sensor LGP2 inhibits TRAF ubiquitin ligase to negatively regulate innate immune signaling.
    Parisien JP, Lenoir JJ, Mandhana R, Rodriguez KR, Qian K, Bruns AM, Horvath CM., Free PMC Article

    04/6/2019
    PACT interacts with LGP2 and this interaction is enhanced by encephalomyocarditis virus (EMCV) infection. In vitro interaction analyses using purified recombinant proteins confirmed that the single-stranded Theiler's murine encephalitis virus genome enhanced the interaction between LGP2 and PACT.

    PACT is required for MDA5-mediated immunoresponses triggered by Cardiovirus infection via interaction with LGP2.
    Miyamoto M, Komuro A.

    11/26/2017
    L region antisense RNA of EMCV is a key determinant of innate immunity to the virus and represents an RNA that activates LGP2 associated MDA5 in virally-infected cells.

    Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells.
    Deddouche S, Goubau D, Rehwinkel J, Chakravarty P, Begum S, Maillard PV, Borg A, Matthews N, Feng Q, van Kuppeveld FJ, Reis e Sousa C., Free PMC Article

    11/28/2015
    This in vivo study reveals that LGP2 is a major downregulator of the influenza A virus-triggered detrimental inflammatory response.

    Protective role of LGP2 in influenza virus pathogenesis.
    Si-Tahar M, Blanc F, Furio L, Chopy D, Balloy V, Lafon M, Chignard M, Fiette L, Langa F, Charneau P, Pothlichet J.

    08/23/2014
    Enhanced expression of LGP2 suppresses the IFN stimulated genes associated with cytotoxic stress by turning off the expression of IFNbeta

    RIG-I-like receptor LGP2 protects tumor cells from ionizing radiation.
    Widau RC, Parekh AD, Ranck MC, Golden DW, Kumar KA, Sood RF, Pitroda SP, Liao Z, Huang X, Darga TE, Xu D, Huang L, Andrade J, Roizman B, Weichselbaum RR, Khodarev NN., Free PMC Article

    05/10/2014
    LGP2, a host protein induced during influenza A virus infection, downregulates the host antiviral IFN response

    LGP2 downregulates interferon production during infection with seasonal human influenza A viruses that activate interferon regulatory factor 3.
    Malur M, Gale M Jr, Krug RM., Free PMC Article

    12/8/2012
    LGP2 promotes an essential prosurvival signal in response to antigen stimulation to confer CD8+ T cell-number expansion and effector functions against divergent RNA viruses, including West Nile virus and lymphocytic choriomeningitis virus.

    The RIG-I-like receptor LGP2 controls CD8(+) T cell survival and fitness.
    Suthar MS, Ramos HJ, Brassil MM, Netland J, Chappell CP, Blahnik G, McMillan A, Diamond MS, Clark EA, Bevan MJ, Gale M Jr., Free PMC Article

    11/24/2012
    findings demonstrate a regulatory role for LGP2 in the response to cytosolic DNA, an intracellular bacterial pathogen, and a DNA virus, and provide a plausible mechanistic hypothesis as the basis for this activity

    Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein.
    Pollpeter D, Komuro A, Barber GN, Horvath CM., Free PMC Article

    09/3/2011
    data suggest that LGP2 facilitates viral RNA recognition by RIG-I and MDA5 through its ATPase domain.

    LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses.
    Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, Tsujimura T, Fujita T, Akira S, Takeuchi O., Free PMC Article

    03/15/2010
    Lgp2 acts as a negative feedback regulator of antiviral signaling by sequestering double-stranded RNA from retinoic acid-inducible gene-I (RIG-I).

    The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I.
    Rothenfusser S, Goutagny N, DiPerna G, Gong M, Monks BG, Schoenemeyer A, Yamamoto M, Akira S, Fitzgerald KA.

    01/21/2010
    Functional analysis of the human LGP2 ortholog.

    RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2.
    Komuro A, Horvath CM., Free PMC Article

    06/19/2007
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