Kyoto University · Medicine
Professor Takashi Fujita's research lab specializes in innate immunology, focusing on the molecular mechanisms underlying antiviral responses and cellular signaling pathways. The lab investigates key pattern recognition receptors such as RIG-I-like receptors and their role in detecting viral RNA, leading to the activation of type I and III interferons. Central to their work is the dissection of signaling cascades involving adaptors like IPS-1, kinases such as TBK-1 and IKK-i, and transcription factors including IRF3/7 and NF-κB. The lab also explores the interplay between transcription factors like Runx2 and signaling pathways such as PI3K-Akt in both development and immune responses.
Figures are computed from collected data and may differ slightly.
Runx2 and phosphatidylinositol 3-kinase (PI3K)-Akt signaling play important roles in osteoblast and chondrocyte differentiation. We investigated the relationship between Runx2 and PI3K-Akt signaling. Forced expression of Runx2 enhanced osteoblastic differentiation of C3H10T1/2 and MC3T3-E1 cells and enhanced chondrogenic differentiation of ATDC5 cells, whereas these effects were blocked by treatment with IGF-I antibody or LY294002 or adenoviral introduction of dominant-negative (dn)-Akt. Forced
Recombinant subunits of the transcription factor NF-kappa B, p50 and p65, were analyzed both for binding to various kappa B motifs and in vitro activation. The subunits preferentially form a heterodimer that activates transcription. Although p50 and p65 bind DNA individually as homodimers and are structurally related, their activation mechanisms are distinct. p65 activates transcription by its unique carboxy-terminal activation domain. (p50)2 displays higher affinity DNA binding than (p65)2 for
Retinoic acid inducible gene I (RIG-I)-like receptors (RLRs) function as cytoplasmic sensors for viral RNA to initiate antiviral responses including type I interferon (IFN) production. It has been unclear how RIG-I encounters and senses viral RNA. To address this issue, we examined intracellular localization of RIG-I in response to viral infection using newly generated anti-RIG-I antibody. Immunohistochemical analysis revealed that RLRs localized in virus-induced granules containing stress granu
Viral infections trigger innate immune responses, including the production of type I interferons (IFN-alpha and -beta) and other proinflammatory cytokines. Novel antiviral cytokines IFN-lambda1, IFN-lambda2, and IFN-lambda3 are classified as type III IFNs and have evolved independently of type I IFNs. Type III IFN genes are regulated at the level of transcription and induced by viral infection. Although the regulatory mechanism of type I IFNs is well elucidated, the expression mechanism of IFN-l
Various cells in the body are capable of sensing infectious viruses and initiating reactions collectively known as antiviral innate responses. These responses include the production of antiviral cytokines such as type I interferon (IFN) 2The abbreviations used are: IFN, interferon; RIG-I, retinoic acid-inducible gene I; RLR, RIG-I-like receptor(s); dsRNA, double-stranded RNA; ssRNA, single-stranded RNA; CARD, caspase recruitment domain; IPS-1, interferon promoter stimulator-1; TRAF3, TNF recepto
Double-stranded RNA or virus triggers a specific signal cascade that results in the activation of the IRF-3/-7 kinase we detected, which corresponds to the long-sought signalling machinery that is responsible for triggering the early phase of innate response. The signal branches to a common NF-kappaB activation cascade, thus resulting in the activation of a set of critical transcription factors for the response.
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