MYB (gene)

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

{{cs1 config|name-list-style=vanc}}

{{Pfam box

|Name=Myb-like DNA-binding domain

|InterPro=IPR001005

|CDD=cd00167

|Symbol=Myb_DNA-binding

|PROSITE=PDOC00037

|Pfam=PF00249

|SCOP=1irz

|CATH=1irz

}}

{{Infobox_gene}}

Myb genes are part of a large gene family of transcription factors found in animals and plants. In humans, it includes Myb proto-oncogene like 1 and Myb-related protein B in addition to MYB proper.{{cite journal |vauthors=Chen Y, Xu H, Liu J, Zhang C, Leutz A, Mo X | title = The c-Myb functions as a downstream target of PDGF-mediated survival signal in vascular smooth muscle cells | journal = Biochem Biophys Res Commun | volume = 360 | issue = 2 | pages = 433–6 | date = Jul 2007 | pmid = 17599807 | doi = 10.1016/j.bbrc.2007.06.078 }}{{cite web | title = Entrez Gene: v-myb myeloblastosis viral oncogene homolog (avian)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4602}} Members of the extended SANT/Myb family also include the SANT domain and other similar all-helical homeobox-like domains.

Function

= Viral=

The Myb gene family is named after the eponymous gene in Avian myeloblastosis virus. The viral Myb (v-Myb, {{UniProt|P01104}}) recognizes the sequence 5'-YAACKG-3'. It causes myeloblastosis (myeloid leukemia) in chickens.{{cite journal | vauthors = Klempnauer KH, Symonds G, Evan GI, Bishop JM | title = Subcellular localization of proteins encoded by oncogenes of avian myeloblastosis virus and avian leukemia virus E26 and by chicken c-myb gene | journal = Cell | volume = 37 | issue = 2 | pages = 537–47 | date = June 1984 | pmid = 6327074 | doi=10.1016/0092-8674(84)90384-2| s2cid = 46196167 }} Compared to the normal animal cellular Myb (c-myb), v-myb contains deletions in the C-terminal regulatory domain, leading to aberrant activation of other oncogenes.{{cite journal | vauthors = George OL, Ness SA | title = Situational awareness: regulation of the myb transcription factor in differentiation, the cell cycle and oncogenesis | journal = Cancers | volume = 6 | issue = 4 | pages = 2049–71 | date = October 2014 | pmid = 25279451 | doi = 10.3390/cancers6042049 | pmc = 4276956 | doi-access = free }}

= Animals =

Myb proto-oncogene protein is a member of the MYB (myeloblastosis) family of transcription factors. The protein contains three domains, an N-terminal DNA-binding domain, a central transcriptional activation domain and a C-terminal domain involved in transcriptional repression. It may play a role in cell cycle regulation. Like the viral version, this gene is an oncogene, and rearrangements of the gene (often involving deletion in the C-terminal domain) causes cancer.

= Plants =

MYB factors represent a family of proteins that include the conserved MYB DNA-binding domain. Plants contain a MYB-protein subfamily that is characterised by the R2R3-type MYB domain.{{cite journal |vauthors=Stracke R, Werber M, Weisshaar B | title = The R2R3-MYB gene family in Arabidopsis thaliana | journal = Curr. Opin. Plant Biol. | volume = 4 | issue = 5 | pages = 447–56 | date = October 2001 | pmid = 11597504 | doi = 10.1016/s1369-5266(00)00199-0 | bibcode = 2001COPB....4..447S }}

In maize, phlobaphenes are synthesized in the flavonoids synthetic pathway{{cite journal |vauthors=Himi E, Mares DJ, Yanagisawa A, Noda K | title = Effect of grain colour gene (R) on grain dormancy and sensitivity of the embryo to abscisic acid (ABA) in wheat | journal = J. Exp. Bot. | volume = 53 | issue = 374 | pages = 1569–74 | date = July 2002 | pmid = 12096095 | doi = 10.1093/jxb/erf005 | doi-access = free }} from polymerisation of flavan-4-ols{{cite journal | author = Winkel-Shirley B | title = Flavonoid biosynthesis. A colorful model for genetics, biochemistry, cell biology, and biotechnology | journal = Plant Physiol. | volume = 126 | issue = 2 | pages = 485–93 | date = June 2001 | pmid = 11402179 | pmc = 1540115 | doi = 10.1104/pp.126.2.485 }}{{cite journal |vauthors=Chopra S, Cocciolone SM, Bushman S, Sangar V, McMullen MD, Peterson T | title = The maize unstable factor for orange1 is a dominant epigenetic modifier of a tissue specifically silent allele of pericarp color1 | journal = Genetics | volume = 163 | issue = 3 | pages = 1135–46 | date = March 2003 | doi = 10.1093/genetics/163.3.1135 | pmid = 12663550 | pmc = 1462483 }} which encodes an R2R3 myb-like transcriptional activator[http://www.intl-pag.org/16/abstracts/PAG16_P05d_343.html Structural And Transcriptional Analysis Of The Complex P1-wr Cluster In Maize. Wolfgang Goettel, Joachim Messing. Plant & Animal Genomes XVI Conference] {{webarchive|url=https://web.archive.org/web/20120218100748/http://www.intl-pag.org/16/abstracts/PAG16_P05d_343.html |date=2012-02-18 }} of the A1 gene encoding for the dihydroflavonol 4-reductase (reducing dihydroflavonols into flavan-4-ols){{cite journal |vauthors=Dong X, Braun EL, Grotewold E | title = Functional conservation of plant secondary metabolic enzymes revealed by complementation of Arabidopsis flavonoid mutants with maize genes | journal = Plant Physiol. | volume = 127 | issue = 1 | pages = 46–57 | date = September 2001 | pmid = 11553733 | pmc = 117961 | doi = 10.1104/pp.127.1.46 | hdl = 1811/48809 | url = http://www.plantphysiol.org/cgi/reprint/127/1/46.pdf }} while another gene (Suppressor of Pericarp Pigmentation 1 or SPP1) acts as a suppressor.{{cite journal | title = Suppressor of Pericarp Pigmentation 1 (SPP1), a novel gene involved in phlobaphene accumulation in maize (Zea mays L.) pericarps. |vauthors=Lee EA, Harper V | journal = Maydica | year = 2002 | volume = 47 | issue = 1 | pages = 51–58 }} {{INIST|13772300}} The maize P gene encodes a Myb homolog that recognizes the sequence CCWACC, in sharp contrast with the YAACGG bound by vertebrate Myb proteins.{{cite journal | vauthors = Grotewold E, Drummond BJ, Bowen B, Peterson T | year = 1994| title = The myb-homologous P gene controls phlobaphene pigmentation in maize floral organs by directly activating a flavonoid biosynthetic gene subset | journal = Cell | volume = 76 | issue = 3| pages = 543–554 | doi = 10.1016/0092-8674(94)90117-1 | pmid = 8313474 | s2cid = 42197232}}

In sorghum, the corresponding yellow seed 1 gene (y1){{cite journal | title = Characterization of a deletion allele of a sorghum Myb gene yellow seedl showing loss of 3-deoxyflavonoids |vauthors=Boddu J, Svabek C, Ibraheem F, Jones AD, Chopra S | journal = Plant Science | year = 2005 | volume = 169 | issue = 3 | pages = 542–552 | doi=10.1016/j.plantsci.2005.05.007|bibcode=2005PlnSc.169..542B }} {{INIST|16983977}} also encodes a R2R3 type of Myb domain protein that regulates the expression of chalcone synthase, chalcone isomerase and dihydroflavonol reductase genes required for the biosynthesis of 3-deoxyflavonoids.{{cite journal |vauthors=Boddu J, Jiang C, Sangar V, Olson T, Peterson T, Chopra S | title = Comparative structural and functional characterization of sorghum and maize duplications containing orthologous myb transcription regulators of 3-deoxyflavonoid biosynthesis | journal = Plant Mol. Biol. | volume = 60 | issue = 2 | pages = 185–99 | date = January 2006 | pmid = 16429259 | doi = 10.1007/s11103-005-3568-1 | s2cid = 23841582 }}

Ruby is a MYB transcriptional activator of genes that produce anthocyanin in citrus fruits. In most citrus varieties Ruby is non-functional, but in blood oranges it upregulates anthocyanin production to produce the characteristic red color of the fruit.{{cite journal |vauthors=Butelli E, Licciardello C, Zhang Y, Liu J, Mackay S, Bailey P, Reforgiato-Recupero G, Martin C | title = Retrotransposons control fruit-specific, cold-dependent accumulation of anthocyanins in blood oranges | journal = Plant Cell | volume = 24 | issue = 3 | pages = 1242–55 | year = 2012 | pmid = 22427337 | pmc = 3336134 | doi = 10.1105/tpc.111.095232 | bibcode = 2012PlanC..24.1242B }}

See also

References

{{Reflist}}

Further reading

{{refbegin | 2}}

  • {{cite journal |vauthors=Oh IH, Reddy EP | title = The myb gene family in cell growth, differentiation and apoptosis. | journal = Oncogene | volume = 18 | issue = 19 | pages = 3017–33 | year = 1999 | pmid = 10378697 | doi = 10.1038/sj.onc.1202839 | doi-access = free }}
  • {{cite journal |vauthors=Nicolaides NC, Gualdi R, Casadevall C, Manzella L, Calabretta B | title = Positive autoregulation of c-myb expression via Myb binding sites in the 5' flanking region of the human c-myb gene. | journal = Mol. Cell. Biol. | volume = 11 | issue = 12 | pages = 6166–76 | year = 1991 | pmid = 1944282 | pmc = 361795 | doi = 10.1128/mcb.11.12.6166-6176.1991}}
  • {{cite journal |vauthors=Kalkbrenner F, Guehmann S, Moelling K | title = Transcriptional activation by human c-myb and v-myb genes. | journal = Oncogene | volume = 5 | issue = 5 | pages = 657–61 | year = 1990 | pmid = 2189102 }}
  • {{cite journal |vauthors=Westin EH, Gorse KM, Clarke MF | title = Alternative splicing of the human c-myb gene. | journal = Oncogene | volume = 5 | issue = 8 | pages = 1117–24 | year = 1990 | pmid = 2202948 }}
  • {{cite journal |vauthors=Dasgupta P, Reddy EP | title = Identification of alternatively spliced transcripts for human c-myb: molecular cloning and sequence analysis of human c-myb exon 9A sequences. | journal = Oncogene | volume = 4 | issue = 12 | pages = 1419–23 | year = 1990 | pmid = 2687764 }}
  • {{cite journal |vauthors=Janssen JW, Vernole P, de Boer PA, Oosterhuis JW, Collard JG | title = Sublocalization of c-myb to 6q21----q23 by in situ hybridization and c-myb expression in a human teratocarcinoma with 6q rearrangements. | journal = Cytogenet. Cell Genet. | volume = 41 | issue = 3 | pages = 129–35 | year = 1986 | pmid = 3007038 | doi = 10.1159/000132217 }}
  • {{cite journal |vauthors=Slamon DJ, Boone TC, Murdock DC, Keith DE, Press MF, Larson RA, Souza LM | title = Studies of the human c-myb gene and its product in human acute leukemias. | journal = Science | volume = 233 | issue = 4761 | pages = 347–51 | year = 1986 | pmid = 3014652 | doi = 10.1126/science.3014652 | bibcode = 1986Sci...233..347S }}
  • {{cite journal |vauthors=Majello B, Kenyon LC, Dalla-Favera R | title = Human c-myb protooncogene: nucleotide sequence of cDNA and organization of the genomic locus. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 83 | issue = 24 | pages = 9636–40 | year = 1987 | pmid = 3540945 | pmc = 387195 | doi = 10.1073/pnas.83.24.9636 | doi-access = free }}
  • {{cite journal |vauthors=Szczylik C, Skorski T, Ku DH, Nicolaides NC, Wen SC, Rudnicka L, Bonati A, Malaguarnera L, Calabretta B | title = Regulation of proliferation and cytokine expression of bone marrow fibroblasts: role of c-myb. | journal = J. Exp. Med. | volume = 178 | issue = 3 | pages = 997–1005 | year = 1993 | pmid = 7688794 | pmc = 2191153 | doi = 10.1084/jem.178.3.997 }}
  • {{cite journal |vauthors=Krieg J, Oelgeschläger M, Janknecht R, Lüscher B | title = High affinity DNA binding of native full length c-Myb and differential proteolytic sensitivity of its N- and C-terminal domains. | journal = Oncogene | volume = 10 | issue = 11 | pages = 2221–8 | year = 1995 | pmid = 7784067 }}
  • {{cite journal |vauthors=Jacobs SM, Gorse KM, Westin EH | title = Identification of a second promoter in the human c-myb proto-oncogene. | journal = Oncogene | volume = 9 | issue = 1 | pages = 227–35 | year = 1994 | pmid = 8302584 }}
  • {{cite journal |vauthors=Favier D, Gonda TJ | title = Detection of proteins that bind to the leucine zipper motif of c-Myb. | journal = Oncogene | volume = 9 | issue = 1 | pages = 305–11 | year = 1994 | pmid = 8302594 }}
  • {{cite journal |vauthors=Glaser R, Lafuse WP, Bonneau RH, Atkinson C, Kiecolt-Glaser JK | title = Stress-associated modulation of proto-oncogene expression in human peripheral blood leukocytes. | journal = Behav. Neurosci. | volume = 107 | issue = 3 | pages = 525–9 | year = 1993 | pmid = 8329139 | doi = 10.1037/0735-7044.107.3.525 }}
  • {{cite journal |vauthors=Dash AB, Orrico FC, Ness SA | title = The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb. | journal = Genes Dev. | volume = 10 | issue = 15 | pages = 1858–69 | year = 1996 | pmid = 8756344 | doi = 10.1101/gad.10.15.1858 | doi-access = free }}
  • {{cite journal |vauthors=Vorbrueggen G, Lovrić J, Moelling K | title = Functional analysis of phosphorylation at serine 532 of human c-Myb by MAP kinase. | journal = Biol. Chem. | volume = 377 | issue = 11 | pages = 721–30 | year = 1997 | pmid = 8960373 | doi = 10.1515/bchm3.1996.377.11.721 }}
  • {{cite journal |vauthors=Tavner FJ, Simpson R, Tashiro S, Favier D, Jenkins NA, Gilbert DJ, Copeland NG, Macmillan EM, Lutwyche J, Keough RA, Ishii S, Gonda TJ | title = Molecular cloning reveals that the p160 Myb-binding protein is a novel, predominantly nucleolar protein which may play a role in transactivation by Myb. | journal = Mol. Cell. Biol. | volume = 18 | issue = 2 | pages = 989–1002 | year = 1998 | pmid = 9447996 | pmc = 108811 | doi = 10.1128/MCB.18.2.989}}
  • {{cite journal |vauthors=Hedge SP, Kumar A, Kurschner C, Shapiro LH | title = c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation. | journal = Mol. Cell. Biol. | volume = 18 | issue = 5 | pages = 2729–37 | year = 1998 | pmid = 9566892 | pmc = 110652 | doi = 10.1128/mcb.18.5.2729}}
  • {{cite journal |vauthors=Leverson JD, Koskinen PJ, Orrico FC, Rainio EM, Jalkanen KJ, Dash AB, Eisenman RN, Ness SA | title = Pim-1 kinase and p100 cooperate to enhance c-Myb activity. | journal = Mol. Cell | volume = 2 | issue = 4 | pages = 417–25 | year = 1998 | pmid = 9809063 | doi = 10.1016/S1097-2765(00)80141-0 | doi-access = free }}
  • {{cite journal |vauthors=Thompson MA, Rosenthal MA, Ellis SL, Friend AJ, Zorbas MI, Whitehead RH, Ramsay RG | title = c-Myb down-regulation is associated with human colon cell differentiation, apoptosis, and decreased Bcl-2 expression. | journal = Cancer Res. | volume = 58 | issue = 22 | pages = 5168–75 | year = 1998 | pmid = 9823328 }}
  • {{cite journal |vauthors=Verbeek W, Gombart AF, Chumakov AM, Müller C, Friedman AD, Koeffler HP | title = C/EBPepsilon directly interacts with the DNA binding domain of c-myb and cooperatively activates transcription of myeloid promoters. | journal = Blood | volume = 93 | issue = 10 | pages = 3327–37 | year = 1999 | pmid = 10233885 | doi = 10.1182/blood.V93.10.3327| doi-access = free }}

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