Nuclear Factor (erythroid-Derived 2)-Like 1 Proteine (NFE2L1)

Human Nuclear Factor (erythroid-Derived 2)-Like 1 (NFE2L1) Interaktionspartner

1. Data show that Nrf1 can adopt several topologies within membranes that are determined by its NTD.

2. Fbw7 as a regulator of Nrf1 expression and reveal a novel function of Fbw7 in cellular stress response.

3. results indicate a novel role of Nrf1 in UVB-induced DNA damage repair and suggest Nrf1 as a tumor suppressor in the skin

4. Data indicate both Nrf1a and Nrf1b isoforms transcripts were detected in different mouse and human cell lines, and in various mouse tissues.

5. Nrf1 knockout resulted in the increased expression of GCLC and GCLM in human bronchial epithelial (HBE1) cells.

6. while Nrf2 is crucial for MRE/ARE-mediated transcription in response to copper, Nrf1 may activate MT-1 expression by a mechanism different from that Nrf2 employs.

7. Nrf1 physically interacts with androgen receptor and enhances it's DNA-binding activity, suggesting that the p65-Nrf1 isoform is a potential androgen receptor coactivator.

8. The treatment with E2, Res, or VC significantly increased mRNA and protein expression levels of Nrf1.

9. The results indicate that Nrf1 is a transcriptional activator of Herpud1 expression during ER stress, and they suggest Nrf1 is a key player in the regulation of the ER stress response in cells.

10. This review outlines Nrf1 structure, function, regulation and its links to insulin resistance, diabetes and inflammation.

11. Importantly, Nrf1 activity is positively and/or negatively regulated by distinct doses of proteasome and calpain inhibitors

12. Together with molecular expression results, the authors thus suppose requirement of Nrf1alpha (and major derivates) for gene regulatory mechanisms repressing cancer cell process and malignant behaviour.

13. These results uncover a new regulatory mechanism that USP15 activates Nrf1 against the beta-TrCP inhibition to maintain proteostasis.

14. Here the authors show that the aspartyl protease DNA-damage inducible 1 homolog 2 (DDI2) is required to cleave and activate Nrf1.

15. Nrf1 is regulated by O-GlcNAc transferase.

16. our investigation shows that the ER membrane protein TCF11/Nrf1 is an essential component of the cellular stress response mechanism. In response to cytotoxic stress, TCF11/Nrf1 is retrotranslocated and transferred to the nucleus where it induces proteasome subunit expression via binding to the ARE region of the relevant promoter.

17. Data uncover an unexpected role for p97 in activation of transcription factor Nrf1 by relocalizing it from the endoplasmic reticulum lumen to the cytosol.

18. Nrf1 is negatively regulated by its O-GlcNAcylation status that depends on the glucose concentrations

19. A proteasome inhibitor-stimulated Nrf1 protein-dependent compensatory increase in proteasome subunit gene expression reduces polycomb group protein level

20. The study identifies casein kinase 2 as an NRF1-binding protein and finds that the knockdown of casein kinase 2 enhances the NRF1-dependent expression of the proteasome subunit genes.

Mouse (Murine) Nuclear Factor (erythroid-Derived 2)-Like 1 (NFE2L1) Interaktionspartner

1. Mechanistic studies revealed that Nfe2l1 deficiency may disturb the expression of lipolytic genes in adipocytes, leading to adipocyte hypertrophy followed by inflammation, pyroptosis, and insulin resistance.

2. our investigation shows that the ER membrane protein TCF11/Nrf1 is an essential component of the cellular stress response mechanism. In response to cytotoxic stress, TCF11/Nrf1 is retrotranslocated and transferred to the nucleus where it induces proteasome subunit expression via binding to the ARE region of the relevant promoter.

3. Deficiency of long isoforms of Nfe2l1 in pancreatic beta-cells increased susceptibility to acute arsenite-induced cytotoxicity by promoting arsenic biotransformation and intracellular MMA levels.

4. Nrf1 is negatively regulated by its O-GlcNAcylation status that depends on the glucose concentrations

5. Denervation induced proteasomal activation via NFE2L1 nuclear translocation in control mice

6. This stduy identify the bZIP transcription factor Nfe2l1 and demonstrate that it promotes glial fate under direct Sox9 regulatory control.

7. The study identifies casein kinase 2 as an NRF1-binding protein and finds that the knockdown of casein kinase 2 enhances the Nrf1-dependent expression of the proteasome subunit genes.

8. Nrf1 plays an integral role in the maintenance of proteasome function in hepatocytes and in the prevention of liver steatosis development.

9. findings suggest that nuclear-related factor erythroid 2 transcription factor (Nrf1) may play a role in maintaining genomic integrity, and that Nrf1 dysregulation may induce tumorigenesis

10. The transcription factor, TCF11, is at the crossroads of oxidative stress and the ubiquitin proteasome system.

11. Data show that nuclear factor erythroid-derived 2-related factor 1 (Nrf1), but not the related Nrf2, is necessary for induced proteasome gene transcription in mouse embryonic fibroblasts.

12. the first in vivo experimental evidence that NFE2L1 produced by osteoblasts is involved in regulating osterix expression, osteoblast differentiation, and bone formation

13. may promote cell survival by maintaining redox balance and protecting embryonic hepatocytes from TNF-mediated apoptosis during development

14. the physical interaction between Nrf1 and C/EBPbeta provide a novel mechanism for the transcriptional regulation of DSPP in odontoblasts.

15. Nrf1 is normally targeted to the endoplasmic reticulum membrane, and endoplasmic reticulum stress may play a role in modulating Nrf1 function as a transcriptional activator

16. Activation of ARE-driven genes by Nrf1 was negatively controlled by the 155-AA N-terminal domain through its ability to direct Nrf1 to the endoplasmic reticulum.

17. Arachidonic acid modulated osterix expression by a mechanism involving Nrf1 nuclear translocation and Nrf1 binding to oxidant response elements to activate genes in cell differentiation.

18. The amino- and carboxyl-terminal regions are required for correct membrane orientation of Nrf1, as deletion of residues 2-10 or 23-30 greatly increase its association with the endoplasmic reticulum and the extent to which it is glycosylated.