Short communicationCloning and mapping of murine Nfe2l1☆
References (14)
- et al.
Basic local alignment search tool
J. Mol. Biol.
(1990) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
Cell
(1986)SPXX, a frequent sequence motif in gene regulatory proteins
J. Mol. Biol.
(1989)- et al.
Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein
Nature
(1993) - et al.
The ubiquitous subunit of erythroid transcription factor NF-E2 is a small basic-leucine zipper protein related to the v-maf oncogene
Proc. Natl. Acad. Sci. USA
(1993) - et al.
Cloning of Nfr1, an NF-E2-related transcription factor by genetic selection in yeast
Proc. Natl. Acad. Sci. USA
(1993) - et al.
Isolation of cDNA encoding the human NF-E2 protein
Proc. Natl. Acad. Sci. USA
(1993)
Cited by (25)
The roles of NFE2L1 in adipocytes: Structural and mechanistic insight from cell and mouse models
2021, Redox BiologyCitation Excerpt :Based on the newest version of Ensembl Genome Browser (http://asia. ensembl.org/index.html), the mouse Nfe2l1 gene maps to the distal end of chromosome 11 [24], spans 12,554 bp DNA, and is divided into 10 exons (Fig. 1) [24]. According to the database, alternative splicing and selective use of translation initiation codons give rise to 12 transcripts (splice variants), resulting in at least two long protein isoforms (L-NFE2L1) containing 741 and 742 amino acids (aa), as well as two short protein isoforms (S-NFE2L1) containing 453 and 583 aa [25,26].
Mechanisms controlling the multistage post-translational processing of endogenous Nrf1α/TCF11 proteins to yield distinct isoforms within the coupled positive and negative feedback circuits
2018, Toxicology and Applied PharmacologyCitation Excerpt :The tricky variations in their abundances could be dependent on different cell types, in which various amounts of Nrf1α and/or TCF11 were differentially expressed and partially processed, leading to distinct profiling of multiple proteaforms, though they had been under similar basal or proteasomal inhibitors-stimulated conditions. Of note, it was found that there exists TCF11 in the normal human and rat, but not mouse, cell lines (Luna et al., 1995; McKie et al., 1995; Novotny et al., 1998; Prieschl et al., 1998), with it being scarcely expressed in cancer cell lines (which was confirmed by sequencing data not shown). In the neuroblastoma SH-SY5Y cells (Fig. S3A), as the doses of MG132, Epox and BTZ increased, abundances of protein-A and/or -C forms of Nrf1 were gradually diminished to their disappearances, then they were replaced by gradually increasing protein-B, along with concomitantly decreasing protein-D isoforms.
NRF1 Is an ER Membrane Sensor that Is Central to Cholesterol Homeostasis
2017, CellCitation Excerpt :As cholesterol is fundamental to virtually all aspects of mammalian biology (Tabas, 2002), it is an appealing teleonomic notion that Nrf1 and SREBP2 co-evolved as a yin-yang counterbalance to stabilize ER-resident metabolic activity (Figure 4E); while both are ER membrane spanning proteins, SREBP2 promotes cholesterol production, whereas Nrf1 promotes cholesterol removal. Finally, as full-length murine Nrf1 is a ubiquitously expressed 741 amino acid protein that is 97% identical to the human ortholog (McKie et al., 1995), a corollary of our discovery is that it may have broad physiological and therapeutic implications. Indeed, pharmacological manipulation of Nrf1 might lead to a new, powerful unifying therapeutic avenue for mitigating the toxic effects of excess cholesterol to treat a multitude of human diseases.
Nuclear Factor Erythroid-2 Like 1 (NFE2L1): Structure, function and regulation
2016, GeneCitation Excerpt :See Fig. 1). The human Nrf1 gene maps to chromosome 17q21.3, whereas the mouse gene is located on the distal end of chromosome 11 (Chan et al., 1995; McKie et al., 1995). Alternative splicing and alternative use of translation initiation codons in the same mRNA molecule produce different sized polypeptides in mouse and human cells.
Changing gears in Nrf1 research, from mechanisms of regulation to its role in disease and prevention
2015, Biochimica et Biophysica Acta - Gene Regulatory MechanismsCitation Excerpt :Both TCF 11 and Nrf1 p120 transactivate genes to similar extents [52,57]. The mouse full-length p120 that is 741 amino acids long, shares 95% sequence identity with human p120, that is 742 amino acids long [52,58]. Full-length Nrf1 contains all of the common regions found in other CNC proteins (ER binding domain, transactivation domain (TAD) and DNA-binding domain (DBD)).
Transcription factor Nrf1 is negatively regulated by its O-GlcNAcylation status
2015, FEBS LettersCitation Excerpt :Almost equal amounts of hNrf1 and TCF11 are expressed in normal human cell lines, whereas human cancer cell lines predominantly express hNrf1 rather than TCF11 (data unpublished in our group). However, these two isoforms have similar transactivation activity mediated primarily by AD1 [47], though the TAD region of Nrf1 lacks the Neh4 subdomain that is present in TCF11 (which is absent in the mouse [48,49]). Herein, we investigated whether the abundance of endogenous TCF 11/hNrf1 is influenced by the O-GlcNAc status.
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The sequence data reported in this paper have been deposited with theEMBL database under Accession No. X78709.