Ask about this productRelated genes to: TOB1 antibody
- Gene:
- TOB1 NIH gene
- Name:
- transducer of ERBB2, 1
- Previous symbol:
- TROB1
- Synonyms:
- TOB, TROB, APRO5
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-01
- Date modifiied:
- 2016-07-04
Related products to: TOB1 antibody
Related articles to: TOB1 antibody
- Elevated sodium concentrations are commonly observed in tumors and sites of inflammation. Previous studies have shown that high salt levels modulate the phenotype and function of CD4 and CD8 T cells, regulatory T cells, and macrophages. In this study, we performed transcriptomic studies that revealed profound alterations in the neutrophil transcriptome upon high salt exposure, with changes that significantly exceeded those triggered by conventional agonists. By integrating transcriptomic data with functional assays, our findings suggest that high salt-induced neutrophil activation involves mitochondrial ROS production, which subsequently activates p38 MAPK and engages FOS-, Bruton's tyrosine kinase (BTK)-, and cyclooxygenase 2 (COX2)-dependent pathways. Remarkably, the plasticity of the neutrophil transcriptome in response to high salt was further evidenced by the upregulation of genes typically associated with other cell types, including semenogelin 1 (), intercellular adhesion molecule-4 (), tripartite motif69 (), amphiregulin (), oncostatin (), and transducer of ERBB2-1 (), suggesting a broader role for neutrophils in different biological processes beyond their participation in innate immunity. - Source: PubMed
Publication date: 2026/01/21
Mazzitelli IgnacioBleichmar LucíaRivelli FedericoFeijoo IngridAdamczyk AlanCabrerizo GonzaloErra Díaz FernandoGeffner Jorge - Due to the growing number of Alzheimer's disease (AD) patients, new drugs are urgently required. A synthetic nonapeptide, JAL-TA9 (YKGSGFRMI), derived from Transducer of ErbB-2.1 (Tob1) protein, cleaves amyloid β (Aβ) 42 with serine protease-like activity. Aβ25-35 was chosen because it is the shortest fragment that forms fibrils and is cytotoxic. Aβ25-35 has been used to create AD model mice, and it appears to be an attractive target for AD therapeutics. Using Thioflavin-T assays, the fluorescence intensity of the reaction of Aβ25-35 and JAL-TA9 was lower than that of Aβ25-35 without JAL-TA9, and the same result was obtained with aggregated Aβ25-35. These data showed that JAL-TA9 inhibits aggregation of Aβ25-35 and dissolves its aggregates. Furthermore, electron microscopy showed that amyloid fibrils of both Aβ25-35 and aggregated Aβ25-35 are reduced in the presence of JAL-TA9. The proteolytic activity of JAL-TA9 against Aβ25-35 was evaluated using HPLC and mass spectrometry. These data showed that JAL-TA9 cleaves both soluble and aggregated forms of Aβ25-35. JAL-TA9 inhibits neuronal cytotoxicity caused by Aβ25-35 aggregation by cleaving Aβ25-35 and its aggregated form. These results suggest that JAL-TA9 is a promising candidate for developing novel drugs against AD. - Source: PubMed
Publication date: 2025/09/03
Nakamura RinaOkada MomokaTakahashi AsukaHayashi YoshihiroKonishi MotomiIto FumiakiMurakami IchiroSaito MotoakiAkizawa Toshifumi - Endoplasmic reticulum stress and glucose supply are significant factors in glioblastoma growth. The present study aims to investigate the impact of glucose-dependent control of , , , , , and gene expression in U87MG glioblastoma cells in response to the inhibition of both enzymatic activities of signaling protein ERN1. The U87MG glioblastoma cells with inhibited both enzymatic activities of ERN1 (endoribonuclease and protein kinase; dnERN1) were used. Cells transfected with an empty vector served as a control. The expression level of the and other genes was studied by quantitative RT-PCR. It was shown that the expression level of the gene is up-regulated, while that of and genes is down-regulated in control glioblastoma cells treated with glucose deprivation. Nevertheless, the ERN1 knockdown modified the sensitivity of and genes to reduced glucose supply. At the same time, the expression of , , and genes in control glioblastoma cells was resistant to glucose deprivation conditions. However, inhibition of the enzymatic activities of ERN1 signaling protein strongly increased the impact of glucose deprivation on gene expression, but down-regulated the expression of the gene. These results demonstrate that the enzymatic activity of signaling protein ERN1 controls the sensitivity of almost all studied genes to glucose deprivation in U87MG glioblastoma cells in a gene-specific manner. This is important for elucidating the endoplasmic reticulum stress-mediated sensitivity of key regulatory gene expression in glioblastoma cells to glucose supply, a significant factor in tumor growth. - Source: PubMed
Publication date: 2025/08/28
Minchenko Oleksandr HViletska Yuliia MSliusar Myroslava YHnatiuk Oksana SRatushna Oksana OFeldman Taia VKozynkevych Halyna EBezrodnyi Borys HMinchenko Dmytro O - Plant growth-promoting rhizobacteria (PGPR) are soil microorganisms through which phytohormones and other bioactive compounds are produced, thereby enhancing plant growth and stress tolerance. In this study, a novel PGPR strain was identified from the rhizosphere of Lycium chinense seedlings, which produce protein-rich fruit. Whole-genome sequencing and annotation revealed that the genome of this strain, designated Pseudomonas sp. A-2, consists of a 6.65-Mb circular chromosome with 5,980 predicted protein-coding sequences. Comparative genomic analysis classified the strain within the genus Pseudomonas. The A-2 strain genome encodes proteins involved in indole-3-acetic acid (IAA) biosynthesis and signaling pathways, which was validated through IAA detection assays and quantitative analyses. Plant growth rates were significantly enhanced by the A-2 strain treatment, with increases of 3-fold in Arabidopsis, 1.5-fold in tobacco, and 1.35-fold in peanut. In Arabidopsis thaliana, expression of key genes associated with lateral and adventitious root formation was induced by the A-2 strain treatment, including ARFs, AMI1, TAA1, YUCs, IBRs, TOB1, and ECH2. Moreover, enhanced tolerance to salt stress was conferred by the A-2 strain treatment, as evidenced by improved biomass accumulation, chlorophyll content, antioxidant enzyme activity, and reduced lipid peroxidation. Levels of total soluble sugars, including trehalose, were elevated in the A-2 strain treated plants, suggesting a role in osmotic adjustment under stress. The plant growth-promoting and stress-alleviating properties of Pseudomonas sp. A-2 highlight its potential application as an effective biological agent for sustainable agriculture. - Source: PubMed
Publication date: 2025/08/19
Lee SangheeKim Young KookNie HualinAhn JongminKim NayoungKo Seo-RinChoi Ah-HyeonKwon HayoungPeng YuxinKwon Suk-YoonShin Ah-Young - Transducer of ErbB2 (TOB) proteins have been shown to promote mRNA decay through interactions with the CCR4-NOT complex and poly(A)-binding protein (PABP). While their role in deadenylation-mediated mRNA degradation is well established, their potential function in translational control remains to be elucidated. Here, we employed an in vitro translation system combined with an RNA tethering strategy to examine the function of TOB1 and TOB2 in translation. Our results demonstrate that TOB1 and TOB2 act as repressors of translation initiation, independent of deadenylation. Notably, this translational repression selectively targets eIF4A-dependent translation, while translation driven by eIF4A-independent IRES elements remains unaffected. While the interaction between TOB proteins and PABP appears to be dispensable, as disruption of this interaction only partially reduces translational repression, the knockdown of CNOT1, the scaffold of the CCR4-NOT complex, substantially relieves this repression, highlighting its indispensable role in the mechanism. Collectively, our findings uncover a previously unrecognized function of TOB proteins as direct repressors of translation initiation, independent of mRNA decay, and highlight a specific reliance on eIF4A activity and CCR4-NOT complex integrity. - Source: PubMed
Miyazaki KanaeTomohiro TakumiFunakami YoshinoriFukao AkiraSuzuki ToruYamamoto TadashiFujiwara Toshinobu