Molecular characterization of Rhodeus uyekii tripartite motif protein 1 (TRIM1) involved in IFN-γ/LPS-induced NF-κB signaling

Kim, Julan; Kim, Dong-Gyun; Nam, Bo‐Hye; Kim, Young‐Ok; Park, Jung Youn; Kong, Hee Jeong

doi:10.1016/j.fsi.2018.05.011

Cited by 9 publications

(5 citation statements)

References 46 publications

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“…Although human MID2 was originally observed to be associated with the microtubule network and localize with microtubules [ 7 , 14 ], our study showed pMID2 was localized in the cell membrane and cytoplasm. The results were consistent with the RuTRIM1/MID2 that formed aggregates in cytoplasmic bodies [ 13 ]. These differences may be related to the differences in sequence variation among the species, cellular environments, or specific functions.…”

Section: Discussionsupporting

confidence: 87%

“…By contrast, the expression of Xenopus MID2 was undetectable at neurula stages, but it had a weak expression in the pineal gland, otic vesicle, and heart tube at the tailbud stages [ 21 ]. Rhodeus uyekii (RuTRIM1/MID2) was abundant in hepatopancreas and spleen, closely related to immune system, suggesting Ru TRIM1/MID2 might have a role in fish immune system [ 13 ]. Possible explanations for the different expression patterns among species include intra-species variation and divergence during developmental stages.…”

Section: Discussionmentioning

confidence: 99%

“…Human MID2 has been reported to induce nuclear factor-κB (NF-κB) and activator protein 1 (AP-1) signaling, thus mediating regulation of immunity [ 12 ]. Rhodeus uyekii TRIM1/MID2 (RuTRIM1/MID2) has been shown to negatively regulate interferon-γ/lipopolysaccharide-induced nuclear NF-κB signaling, and may play a role in the inflammatory response [ 13 ]. These findings imply MID2 might be involved in the regulation of innate immunity.…”

Section: Introductionmentioning

confidence: 99%

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The Molecular and Function Characterization of Porcine MID2

Chen,

Zhou,

Yang

et al. 2023

Animals

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Midline2 (MID2/TRIM1) is a member of the tripartite motif-containing (TRIM) family, which is involved in a wide range of cellular processes. However, fundamental studies on porcine MID2 (pMID2) are still lacking. In this study, we identified and characterized the full length MID2 gene of pig (Sus scrofa). The sequence alignment analysis results showed that pMID2 had an N-terminal RING zinc-finger domain, BBC domain, and C-terminal COS box, FN3 motif, and PRY-SPRY domain that were conserved and similar to those of other vertebrates. Furthermore, pMID2 had the highest expression levels in porcine lung and spleen. Serial deletion and site-directed mutagenesis showed that the putative nuclear factor-κB (NF-κB) binding site may be an essential transcription factor for regulating the transcription expression of pMID2. Furthermore, the immunofluorescence assay indicated that pMID2 presented in the cell membrane and cytoplasm. To further study the functions of pMID2, we identified and determined its potential ability to perceive poly (I:C) and IFN-α stimulation. Stimulation experiments showed pMID2 enhanced poly (I:C)-/IFN-α-induced JAK-STAT signaling pathway, indicating that pMID2 might participate in the immune responses. In conclusion, we systematically and comprehensively analyzed the characterizations and functions of pMID2, which provide valuable information to explore the pMID2 functions in innate immunity. Our findings not only enrich the current knowledge of MID2 in IFN signaling regulation but also offer the basis for future research of pig MID2 gene.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Molecular and Function Characterization of Porcine MID2

Chen,

Zhou,

Yang

et al. 2023

Animals

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“…TRIM family is closely associated with the activation of the NF-κB signaling pathway due to its conserved RBCC structure, especially the RING structure, which gives it E3 ubiquitin ligase activity (23)(24)(25). The regulation of the TRIMs for the NF-κB signaling pathway is diverse, and some members of the triple structural domain protein family are involved in the activation of the NF-κB signaling pathway, for example, TRIM1 is involved in the tumor necrosis factor (TNF) α/LPS-induced activation of the NF-κB signaling pathway (26), TRIM52 acts as a positive regulator to regulate the NF-κB signaling pathway (27), and TRIM22 also has an activating effect on the NF-κB signaling pathway (28). It has been reported that TRIM22/ activates NF-κB signaling in glioblastoma by accelerating the degradation of IκBα (29); TRIM47 activates NF-κB signaling via PKC-ε/PKD3 stabilization and contributes to endocrine therapy resistance in breast cancer (30), and TRIM10 activates the NF-κB signaling pathway in osteosarcoma (31).…”

Section: Discussionmentioning

confidence: 99%

Tripartite motif 52 (TRIM52) promotes proliferation, migration, and regulation of colon cancer cells associated with the NF-κB signaling pathway

Guo¹,

Zhou²,

Gu³

et al. 2022

J Gastrointest Oncol

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Background: With the advancement of early detection and treatment, the incidence of colon cancer (CC) has declined steadily worldwide; however, the mortality remains unacceptably high. Tripartite motif 52 (TRIM52) is a member of the family of highly conserved RBCC (a RING-finger, two B-boxes, and a predicted alpha-helical Coiled-Coil domain were linked to the N-terminal region in sequence) proteins with more than 70 isoforms, which plays an important role in tumorigenesis through different signaling pathways.How it regulates the development of CC remains unknown.Methods: Western blot was used to reveal that TRIM52 protein expression is up-regulated in CC cells.The Analysis of The Cancer Genome Atlas (TCGA) database was used to find the different expressions of TRIM52 between colon cancer tissues and normal colonic epithelial tissues. Cell proliferation assays, migration and invasion assays, and apoptosis were used to verify the changes in cell function after knockdown or overexpression of TRIM52 in CC cells. After that, the key proteins of the nuclear factor (NF)-κB signaling pathway were validated by western blot to explore the role of TRIM52 in the NF-κB signaling pathway.Finally, in order to explore the potential sites of TRIM52, LPS and PDTC were employed to activate and block the NF-κB signaling pathway, and the key proteins of the NF-κB signaling pathway were validated by western blot.Results: TGCA database revealed that TRIM52 expression was elevated in CC tissues and correlated with prognosis. It was verified that TRIM52 promoted the proliferation, migration, and invasion of CC cells, and inhibited cell apoptosis. Most of the tripartite motif proteins (TRIMs) have ubiquitin ligase activity related to their highly conserved RING structure. Detection of the key proteins of the NF-κB signaling pathway in CC cells revealed that TRIM52 activated the NF-κB signaling pathway. Conclusions:We confirmed that TRIM52 promotes proliferation, migration, and invasion while inhibiting apoptosis of CC cells. The regulatory effect of TRIM52 on CC cells is related to the activation of the NF-κB signaling pathway. As TRIM52 acted as an upstream stimulator, stimulating the transfer of P65 into the nucleus to activate the NF-κB signaling pathway, it may provide a potential target for prognosis prediction and treatment of CC.

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“…These TRIM-like proteins exclusively identified in the fish were called fish novel TRIMs (finTRIMs). Nevertheless, although increasing data support the immunomodulatory potential of fish TRIMs against microbial infections [17,22], the molecular determinants associated with their antimicrobial mechanisms are still being investigated in cellular and animal models.…”

Section: Introductionmentioning

confidence: 99%

Novel TRIM Proteins Involved in Rainbow Trout Innate Immune Response

Donoso,

Ramírez-Cepeda,

Salinas-Parra

et al. 2024

Preprint

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In mammals, Tripartite motif-containing (TRIM) proteins modulate the immune response by coordinating pro-inflammatory related processes such as antiviral restriction, cellular autophagy and inflammasome activation. In fish, TRIM proteins have been reported mainly in cyprinids (e.g., carp, zebrafish) and salmonids (rainbow trout). However, their molecular mechanisms and functions are still being described these animals. Our study focused on characterizing novel TRIM proteins involved in the innate immune response of gill cells from rainbow trout stimulated with LPS or poly(I:C). Also, a fish trial was performed to detect TRIM proteins of rainbow trout after a challenge with Flavobacterium psychrophilum, a salmonid bacterial pathogen. At in vitro level, the results showed that, among several TRIM proteins, OmTRIM25 triggered an LPS-induced expression of pro-inflammatory cytokines (TNF-α2 and IL-1β), suggesting a potential local modulatory function. Moreover, in the fish trial, while OmTRIM25 and finTRIM2 were up-regulated in the gills two days post infection (dpi), IL-1β and TNF-α2 reached their peaks of expression at four- and six-dpi. Finally, after delving into the function of OmTRIM25 by RNA interference (RNAi) gene-silencing, we propose that TRIM proteins such as OmTRIM25 are needed to induce the pro-inflammatory response in the gills of rainbow trout, which confirms their immunomodulatory function.

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Molecular characterization of Rhodeus uyekii tripartite motif protein 1 (TRIM1) involved in IFN-γ/LPS-induced NF-κB signaling

Cited by 9 publications

References 46 publications

The Molecular and Function Characterization of Porcine MID2

The Molecular and Function Characterization of Porcine MID2

Tripartite motif 52 (TRIM52) promotes proliferation, migration, and regulation of colon cancer cells associated with the NF-κB signaling pathway

Novel TRIM Proteins Involved in Rainbow Trout Innate Immune Response

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