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Data suggest a central role of XBP1 in TLR7 (show TLR7 Proteins)-induced IFNalpha production and identify XBP1 as a potential novel therapeutic target in IFNalpha-driven autoimmune and inflammatory diseases.
the XBP1u nascent chain is transferred from the signal recognition particle to the translocon; however, it cannot pass through the translocon or insert into the membrane.
The biologic processes altered by aberrant IRE1alpha (show ERN1 Proteins)-XBP1 signaling in these innate immune cells.
MiR (show MLXIP Proteins)-665 induced apoptosis by inhibiting XBP1 and ORMDL3 (show ORMDL3 Proteins).
IRE1alpha (show ERN1 Proteins) was shown to cleave miR (show MLXIP Proteins)-150 and thereby to release the suppressive effect that miR (show MLXIP Proteins)-150 exerted on alphaSMA (show ACTA2 Proteins) expression through c-Myb (show MYB Proteins). Inhibition of IRE1alpha (show ERN1 Proteins) was also demonstrated to block endoplasmic reticulum expansion through an XBP-1-dependent pathway.
mTORC2 (show CRTC2 Proteins) responds to glutamine (show GFPT1 Proteins) catabolite levels to modulate the hexosamine biosynthesis enzyme GFAT1 (show GFPT1 Proteins), and is essential for proper expression and nuclear accumulation of the GFAT1 (show GFPT1 Proteins) transcriptional regulator, Xbp1s.
we identify a positive feedback regulatory loop consisting of XBP1 and NCOA3 (show NCOA3 Proteins) that maintains high levels of NCOA3 (show NCOA3 Proteins) and XBP1 expression in breast cancer tissues.
The findings indicate that IRE1 (show ERN1 Proteins)-XBP1 downregulation distinguishes germinal center B-cell-like diffuse large B-cell lymphoma (DLBCL) from other DLBCL subtypes and contributes to tumor growth.
XBP1 does not act as a direct activator of STAT3 phosphorylation. Hence, in regenerati (show DDR1 Proteins)ng livers, XBP1 deficiency most likely affects STAT3 phosphorylation in an indirect manner, possibly related to unresolved ER stress.
reciprocal regulation of Pin1 (show PIN1 Proteins) and XBP1s is associated with the activation of oncogenic pathways, and the relationship of PIN1 (show PIN1 Proteins) and XBP1 may be an attractive target for novel therapy in cancers
one of the antioxidant enzymes, Prdx-2 (show PRDX2 Proteins), was abundantly nitrosylated and temporarily reduced in antioxidant activity, causing transient endogenous hydrogen peroxide (H2O2) accumulation and subsequent X-box binding protein-1s/phosphatidylinositol 3-kinase pathway activation.Prdx-2 nitrosylation could be a potent strategy to affect the pluripotent stem cell-derived cardiomyogenesis.
XBP1 deficiency in smooth muscle cells caused VSMC dedifferentiation and aggravated aortic aneurysms. XBP1u directly associated with the N terminus of FoxO4 (show FOXO4 Proteins).
Data show that LPS (show TLR4 Proteins) induces endoplasmic reticulum (ER) stress and P300 (show NOTCH1 Proteins) activity via the XBP1/IRE1 (show ERN1 Proteins) pathway.
Data suggest that activation of GRP78 (show HSPA5 Proteins)/Ire1 (show ERN1 Proteins)/Xbp1 pathway of ER stress-unfolded protein response is involved in mouse decidualization.
insulin (show INS Proteins) and aPC (show APC Proteins) converge on a common spliced-X-box binding protein-1 (sXBP1) signaling pathway to maintain endoplasmic reticulum (ER) homeostasis.
although feeding LS-Xbp1(-/-) mice cholesterol did not increase CYP7A1 (show CYP7A1 Proteins) expression, serum C4 levels increased significantly up to levels similar to chow-fed Xbp1(fl/fl (show FLT3LG Proteins)) mice and the total bile acid pool normalized. In conclusion, loss of hepatic XBP1 decreased the bile acid pool and CYP7A1 (show CYP7A1 Proteins) synthetic activity.
However, depletion of XBP1 and ATF6 (show ATF6 Proteins), alone or in combination, prevented autophagy induction and significantly enhanced Japanese encephalitis virus-induced cell death.
XBP1 expression regulates the unfolded protein response, acute-phase response, and DDR (show DDR1 Proteins) in hepatocytes. In regenerating livers, XBP1 deficiency leads to endoplasmic reticulum stress and DNA damage.
analyzed XBP1 level and location to explore the effect of ER stress on oocyte maturation and developmental competency of porcine embryos in an in vitro culture system
Knock-down of XBP1 enhanced endoplasmic reticulum stress-mediated cell death in porcine embryonic fibroblasts.
Exposure of endothelial cells to VEGF (show VEGFA Proteins), high glucose, or hydrogen peroxide up-regulated the XBP1/IRE1 alpha (show ERN1 Proteins) and ATF6 (show ATF6 Proteins) arms of the unfolded protein response compared with untreated cells.
Expression of xbp1 is significantly upregulated in the liver of Cdipt (show CDIPT Proteins)-deficient zebrafish due to persistent endoplasmic reticulum stress. Cdipt (show CDIPT Proteins)-deficient zebrafish exhibits hepatic lipid accumulation.
zebrafish XBP-1 spliced form not only activates genes responsible for protein folding, transporting, glycosylation and Endoplasmic Reticulum associated degradation but also activates anti-apoptosis signal via IGF1 (show IGF1 Proteins)/Akt (show AKT1 Proteins) pathway in unfolded protein
XBP1 might function as an inhibitor of mesodermal and neural tissue formation by acting either as transcriptional activator or as repressor.
This gene encodes a transcription factor that regulates MHC class II genes by binding to a promoter element referred to as an X box. This gene product is a bZIP protein, which was also identified as a cellular transcription factor that binds to an enhancer in the promoter of the T cell leukemia virus type 1 promoter. It may increase expression of viral proteins by acting as the DNA binding partner of a viral transactivator. It has been found that upon accumulation of unfolded proteins in the endoplasmic reticulum (ER), the mRNA of this gene is processed to an active form by an unconventional splicing mechanism that is mediated by the endonuclease inositol-requiring enzyme 1 (IRE1). The resulting loss of 26 nt from the spliced mRNA causes a frame-shift and an isoform XBP1(S), which is the functionally active transcription factor. The isoform encoded by the unspliced mRNA, XBP1(U), is constitutively expressed, and thought to function as a negative feedback regulator of XBP1(S), which shuts off transcription of target genes during the recovery phase of ER stress. A pseudogene of XBP1 has been identified and localized to chromosome 5.
X-box binding protein 1 pseudogene 1
, X-box binding protein pseudogene 1
, X-box binding protein 1
, X-box-binding protein 1
, tax-responsive element-binding protein 5
, tax-responsive element-binding protein 5 homolog
, hepatocarcinogenesis-related transcription factor
, X-box binding protein 1B