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- Table of Contents
2 Citations 17 Q&As
1 Citations 5 Q&As
Facts about X-box-binding protein 1.
Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins (PubMed:11460154). Modulates the cellular response to ER stress in a PIK3R-dependent way (PubMed:20348923).
Human | |
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Gene Name: | XBP1 |
Uniprot: | P17861 |
Entrez: | 7494 |
Belongs to: |
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bZIP family |
HTF; TREB5; X-box binding protein 1; X-box-binding protein 1; XBP1; XBP-1; XBP2; XBP2Tax-responsive element-binding protein 5
Mass (kDA):
28.695 kDA
Human | |
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Location: | 22q12.1|22q12 |
Sequence: | 22; NC_000022.11 (28794560..28800572, complement) |
Expressed in plasma cells in rheumatoid synovium (PubMed:11460154). Over-expressed in primary breast cancer and metastatic breast cancer cells (PubMed:25280941). Isoform 1 and isoform 2 are expressed at higher level in proliferating as compared to confluent quiescent endothelial cells (PubMed:19416856).
Endoplasmic reticulum. Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubMed:23529610).; [Isoform 1]: Nucleus. Cytoplasm. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Membrane; Peripheral membrane protein. Shows no preferential localization to either the nucleus or the cytoplasm (By similarity). Shuttles between the nucleus and the cytoplasm in a CRM1-dependent manner (PubMed:16461360). Localizes predominantly at
XBP1 is a gene that encodes a transcription factor involved in ER-associated degradation and host stress responses. The gene is spliced, and is regulated by IRE1. This article discusses how XBP1 targets genes and its potential uses. In addition, it covers IRE1 and its function in splicing. This article is meant for scientists, not for laypeople.
The IRE1 gene encodes a protein that is highly expressed in the liver. It is involved in the regulation of many physiological processes, including the production of energy and growth. When it is expressed in human cells, the IRE1 gene may play a role in tumor growth. The IRE1 gene has been used to test for tumors for a number of years. It is a valuable marker for research and development.
The IRE1 gene encodes a single-pass ER transmembrane protein. It undergoes autophosphorylation and oligomerization. This gene regulates RNase activity and initiates productive splicing of XBP1 mRNA. The IRE1 gene is essential for the replication of coronaviruses, which is why it is so widely used in the field of infectious disease research.
IRE1 is involved in the unfolded protein response. This pathway is related to innate immune functions, inflammatory signal transduction, and regulated IRE1 a-dependent decay. However, it has not been linked to autophagy. Inhibition of BCAT1 inhibits the expression of IRE1.
The XBP1 marker is an excellent tool to identify genes that regulate cell-cycle regulation. In this study, we used a mouse XBP1 plasmid to identify genes involved in protein folding, secretion, and Th2 cell activation. Moreover, we also examined XBP1's role in regulating gene expression in human lymphoblasts.
To identify the targets of XBP1, we performed ChIP-seq analysis. We identified several binding events in the promoter regions of known target genes. These regions included intronic and promoter regions, as well as intergenic regions. Our analysis revealed that XBP1 binds to both promoters and potential enhancers. In addition, we looked at interactions between XBP1 and other known transcription factors in the STRING database.
XBP1 has been shown to be an important transcription factor involved in T helper cell differentiation. Furthermore, it is essential for dendritic cell survival and differentiation. It has been shown to interfere with normal physiological Th2 activation and regulate the cytokine secretion. It is important to note that more in vivo studies are necessary to understand the role of XBP1 in the regulation of the immune response.
Using a proprietary gene expression assay, we characterized XBP1 target genes in human primary HSCs. The results showed that overexpression of the XBP1 protein stimulated the ER chaperone protein BiP, which in turn may be involved in ER stress. Moreover, XBP1 expression induced fibrogenesis in primary human HSCs and two human HSC cell lines.
In mouse liver disease, XBP1 co-induced gene signatures in a variety of tissues. We used primary HSCs (HSCs) that were culture-activated and in vivo treated with a high-fat cholesterol diet. We also assessed disease progression by categorizing liver tissues by the presence of XBP1 or its protein. The heatmap depicts enrichment p-values for gene sets.
XBP1 is involved in cell proliferation, which facilitates the rapid expansion of activated Th2 cells. It also plays a role in cytokine production, thereby facilitating controlled expansion of Th2 cells. As a result, XBP1 has the potential to regulate these processes. This is important because it may play a role in regulating the cell cycle, which is a hallmark of human cancer.
IRE1a-XBP1 pathway has been implicated in autophagy and is associated with the activation of fibrotic HSCs. This pathway also modulates glucose homeostasis and is functionally connected to autophagy. Further, it may be important to understand the role of XBP1 in regulating HSC activation. The role of XBP1 in regulating cell proliferation and metabolism has been demonstrated in other cell types. However, future studies should determine whether XBP1 is also involved in the activation of HSCs.
XBP1 splicing in the Boster Bio assay is performed by inducing a change in XBP1 expression. In vivo, XBP1 levels are higher than in vitro, so it is likely that a treatment with MKC-3946 will lead to enhanced cytotoxicity. In the present study, we show that MKC-3946 inhibits XBP1 splicing and increases cellular cytotoxicity in a dose-dependent manner.
XBP1-u controls the MDM2/p53 axis, a crucial regulatory pathway in the cell cycle and senescence. Hence, it has a wide-ranging influence on the cellular cytokine landscape and reveals a novel role in pivotal biological functions. The current study shows that XBP1 splicing in Boster Bio provides an important new insight into the function of MDM2/p53.
IRE1a mediates XBP1 splicing, and our study showed that overexpression of this protein activates the RNase activity of IRE1. In HEMn-MP cells, IRE1a overexpression dramatically increased XBP1 splicing, as did overexpression in Mel-RMu cells. Further, 4m8C inhibits IRE1a, which prevents XBP1 splicing.
IRE1 catalyzes the non-conventional cytosolic splicing of XBP1 mRNA. IRE1 cuts out a 26-nt intron from mRNA. This creates an active spliced form of XBP1 mRNA, which is essential for the UPR program. In this manner, IRE1 modulates the ER protein-folding capacity of the cell.
In a recent study, researchers found that a gene called XBP1 is upregulated during T helper cell differentiation. They used this marker to detect this gene's expression. The results showed that this gene has an impact on cell proliferation in both Th2 and T2 cells. Specifically, this gene is upregulated in T-helper cells, and is associated with better PFS and OS than in Th2 cells.
This marker is required for the biogenesis of the exocrine gland machinery and regulates a subset of chaperone genes involved in the unfolded protein response. Moreover, it links ER stress to intestinal inflammation. Thus, it is an important gene for research on inflammatory bowel disease and is associated with an increased risk for the development of the disease. However, its role is not well understood.
This gene is a key regulator of several processes. XBP1 regulates ER stress and signals the growth of plasma cells and hepatocytes. Additionally, it regulates transcription factors and signal transduction in B cells. XBP1 is also involved in liver lipogenesis. Its expression is a useful biomarker for studying a disease in this organ. It has been found to be useful in a variety of applications, from detecting cancer cells to discovering genetic variants associated with susceptibility to MAFD7.
The XBP1 gene is also known to regulate Blimp1, a transcription factor that binds to the ER. In fact, its expression is up-regulated by the XBP1 gene in B cells after LPS stimulation. In addition, Blimp1 and IRF4 mRNAs were overexpressed in these cells, suggesting that the XBP1 gene regulates PC development.
A new study reveals a role for XBP1 in UPR signaling. By regulating the expression of ERdj4 and CHOP, XBP-1 can enhance the efficiency of the UPR signaling pathway. Transfection of cotransfected XBP-1s with Tm or MG-132 inhibits IRE1a-mediated proteolysis and induces XBP-1u and XBP-1s protein synthesis. Furthermore, cotransfection of XBP-1s with ERdj4 promoters resulted in transactivation of ERdj4 promoter.
XBP1 regulates the mammalian unfolded protein response (UPR) that protects the ER from misfolded proteins. We identified several XBP-1 target genes in cell lines, including the DnaJ/Hsp40-like gene DnaJ, ERdj4, and p58IPK DnaJ/Hsp40. Additionally, XBP-1 regulates ribosome-associated membrane protein 4 (RAMP-A).
Activation of the IRE1-XBP1 signaling pathway has been associated with cancer development. Mutations in XBP1 result in poorer prognosis. This pathway is implicated in chemoresistance, and activation of XBP1 regulates cancer-infiltrating immune cells. In addition, overexpression of XBP1 has been linked to increased tumorgenesis and poorer survival in EsR-positive breast cancer.
XBP1 is essential for tumor development and progression. It induces plasma cell differentiation, promotes tumorigenesis, and increases drug resistance. It inhibits apoptosis and interacts with multiple signaling pathways. It has been shown that XBP-1 regulates some UPR target genes, while having no effect on others. And yet, many tumors show a significant inverse correlation with XBP1 expression.
PMID: 2321018 by Liou H.-C., et al. A new member of the leucine zipper class of proteins that binds to the HLA DR alpha promoter.
PMID: 2196176 by Yoshimura T., et al. Multiple cDNA clones encoding nuclear proteins that bind to the tax- dependent enhancer of HTLV-1: all contain a leucine zipper structure and basic amino acid domain.
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