GRLF1

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Glucocorticoid receptor DNA-binding factor 1 is a protein that in humans is encoded by the GRLF1 gene.{{cite journal | vauthors = LeClerc S, Palaniswami R, Xie BX, Govindan MV | title = Molecular cloning and characterization of a factor that binds the human glucocorticoid receptor gene and represses its expression | journal = The Journal of Biological Chemistry | volume = 266 | issue = 26 | pages = 17333–40 | date = Sep 1991 | doi = 10.1016/S0021-9258(19)47378-X | pmid = 1894621 | doi-access = free }}{{cite web | title = Entrez Gene: GRLF1 glucocorticoid receptor DNA binding factor 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2909}}

Function

The human glucocorticoid receptor DNA binding factor, which associates with the promoter region of the glucocorticoid receptor gene (hGR gene), is a repressor of glucocorticoid receptor transcription. The amino acid sequence deduced from the cDNA sequences show the presence of three sequence motifs characteristic of a zinc finger and one motif suggestive of a leucine zipper in which 1 cysteine is found instead of all leucines. The GRLF1 enhances the homologous down-regulation of wild-type hGR gene expression. Biochemical analysis suggests that GRLF1 interaction is sequence specific and that transcriptional efficacy of GRLF1 is regulated through its interaction with specific sequence motif. The level of expression is regulated by glucocorticoids.

References

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Further reading

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  • {{cite journal | vauthors = Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T | title = Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones | journal = DNA Research | volume = 9 | issue = 3 | pages = 99–106 | date = Jun 2002 | pmid = 12168954 | doi = 10.1093/dnares/9.3.99 | doi-access = free }}
  • {{cite journal | vauthors = Warriar N, Pagé N, Govindan MV | title = Expression of human glucocorticoid receptor gene and interaction of nuclear proteins with the transcriptional control element | journal = The Journal of Biological Chemistry | volume = 271 | issue = 31 | pages = 18662–71 | date = Aug 1996 | pmid = 8702520 | doi = 10.1074/jbc.271.31.18662 | doi-access = free }}
  • {{cite journal | vauthors = Tikoo A, Czekay S, Viars C, White S, Heath JK, Arden K, Maruta H | title = p190-A, a human tumor suppressor gene, maps to the chromosomal region 19q13.3 that is reportedly deleted in some gliomas | journal = Gene | volume = 257 | issue = 1 | pages = 23–31 | date = Oct 2000 | pmid = 11054565 | doi = 10.1016/S0378-1119(00)00387-5 }}
  • {{cite journal | vauthors = Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Research | volume = 7 | issue = 6 | pages = 347–55 | date = Dec 2000 | pmid = 11214970 | doi = 10.1093/dnares/7.6.347 | doi-access = free }}
  • {{cite journal | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 | bibcode = 2004PNAS..10112130B | doi-access = free }}
  • {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nature Biotechnology | volume = 23 | issue = 1 | pages = 94–101 | date = Jan 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 | s2cid = 7200157 }}
  • {{cite journal | vauthors = Barberis D, Casazza A, Sordella R, Corso S, Artigiani S, Settleman J, Comoglio PM, Tamagnone L | title = p190 Rho-GTPase activating protein associates with plexins and it is required for semaphorin signalling | journal = Journal of Cell Science | volume = 118 | issue = Pt 20 | pages = 4689–700 | date = Oct 2005 | pmid = 16188938 | doi = 10.1242/jcs.02590 | s2cid = 15559113 | url = http://repository.cshl.edu/22532/1/Sordella%20J%20Cell%20Sci%202005.pdf | doi-access = free }}
  • {{cite journal | vauthors = Holinstat M, Knezevic N, Broman M, Samarel AM, Malik AB, Mehta D | title = Suppression of RhoA activity by focal adhesion kinase-induced activation of p190RhoGAP: role in regulation of endothelial permeability | journal = The Journal of Biological Chemistry | volume = 281 | issue = 4 | pages = 2296–305 | date = Jan 2006 | pmid = 16308318 | doi = 10.1074/jbc.M511248200 | doi-access = free }}
  • {{cite journal | vauthors = Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, Kim JM, Song KS, Noh SM, Kim S, Yoo HS, Kim YS, Kim NS | title = Transcriptome analysis of human gastric cancer | journal = Mammalian Genome | volume = 16 | issue = 12 | pages = 942–54 | date = Dec 2005 | pmid = 16341674 | doi = 10.1007/s00335-005-0075-2 | s2cid = 69278 }}
  • {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 | s2cid = 7827573 | doi-access = free }}
  • {{cite journal | vauthors = Mammoto T, Parikh SM, Mammoto A, Gallagher D, Chan B, Mostoslavsky G, Ingber DE, Sukhatme VP | title = Angiopoietin-1 requires p190 RhoGAP to protect against vascular leakage in vivo | journal = The Journal of Biological Chemistry | volume = 282 | issue = 33 | pages = 23910–8 | date = Aug 2007 | pmid = 17562701 | doi = 10.1074/jbc.M702169200 | doi-access = free }}

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