The Myb gene family is named after the eponymous gene in
Avian myeloblastosis virus. The viral Myb (v-Myb, P01104) recognizes the sequence 5'-
YAAC
KG-3'. It causes myeloblastosis (myeloid leukemia) in chickens.[7] 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.[8]
Animals
Myb proto-oncogene protein is a member of the MYB (myeloblastosis) family of
transcription factors. The protein contains three domains, an
N-terminalDNA-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.[8]
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.[9]
In maize,
phlobaphenes are synthesized in the flavonoids synthetic pathway[10] from polymerisation of
flavan-4-ols[11][12] which encodes an R2R3 myb-like
transcriptional activator[13] of the A1 gene encoding for the
dihydroflavonol 4-reductase (reducing
dihydroflavonols into flavan-4-ols)[14] while another gene (Suppressor of Pericarp Pigmentation 1 or SPP1) acts as a
suppressor.[15] The maize P gene encodes a Myb homolog that recognizes the sequence CCWACC, in sharp contrast with the YAACGG bound by vertebrate Myb proteins.[16]
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.[19]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Chen Y, Xu H, Liu J, Zhang C, Leutz A, Mo X (Jul 2007). "The c-Myb functions as a downstream target of PDGF-mediated survival signal in vascular smooth muscle cells". Biochem Biophys Res Commun. 360 (2): 433–6.
doi:
10.1016/j.bbrc.2007.06.078.
PMID17599807.
^Lee EA, Harper V (2002). "Suppressor of Pericarp Pigmentation 1 (SPP1), a novel gene involved in phlobaphene accumulation in maize (Zea mays L.) pericarps". Maydica. 47 (1): 51–58.
INIST13772300
^Grotewold E, Drummond BJ, Bowen B, Peterson T (1994). "The myb-homologous P gene controls phlobaphene pigmentation in maize floral organs by directly activating a flavonoid biosynthetic gene subset". Cell. 76 (3): 543–554.
doi:
10.1016/0092-8674(94)90117-1.
PMID8313474.
S2CID42197232.
^Boddu J, Svabek C, Ibraheem F, Jones AD, Chopra S (2005). "Characterization of a deletion allele of a sorghum Myb gene yellow seedl showing loss of 3-deoxyflavonoids". Plant Science. 169 (3): 542–552.
doi:
10.1016/j.plantsci.2005.05.007.
INIST16983977
^Boddu J, Jiang C, Sangar V, Olson T, Peterson T, Chopra S (January 2006). "Comparative structural and functional characterization of sorghum and maize duplications containing orthologous myb transcription regulators of 3-deoxyflavonoid biosynthesis". Plant Mol. Biol. 60 (2): 185–99.
doi:
10.1007/s11103-005-3568-1.
PMID16429259.
S2CID23841582.
Kalkbrenner F, Guehmann S, Moelling K (1990). "Transcriptional activation by human c-myb and v-myb genes". Oncogene. 5 (5): 657–61.
PMID2189102.
Westin EH, Gorse KM, Clarke MF (1990). "Alternative splicing of the human c-myb gene". Oncogene. 5 (8): 1117–24.
PMID2202948.
Dasgupta P, Reddy EP (1990). "Identification of alternatively spliced transcripts for human c-myb: molecular cloning and sequence analysis of human c-myb exon 9A sequences". Oncogene. 4 (12): 1419–23.
PMID2687764.
Janssen JW, Vernole P, de Boer PA, Oosterhuis JW, Collard JG (1986). "Sublocalization of c-myb to 6q21----q23 by in situ hybridization and c-myb expression in a human teratocarcinoma with 6q rearrangements". Cytogenet. Cell Genet. 41 (3): 129–35.
doi:
10.1159/000132217.
PMID3007038.
Slamon DJ, Boone TC, Murdock DC, Keith DE, Press MF, Larson RA, Souza LM (1986). "Studies of the human c-myb gene and its product in human acute leukemias". Science. 233 (4761): 347–51.
Bibcode:
1986Sci...233..347S.
doi:
10.1126/science.3014652.
PMID3014652.
Krieg J, Oelgeschläger M, Janknecht R, Lüscher B (1995). "High affinity DNA binding of native full length c-Myb and differential proteolytic sensitivity of its N- and C-terminal domains". Oncogene. 10 (11): 2221–8.
PMID7784067.
Jacobs SM, Gorse KM, Westin EH (1994). "Identification of a second promoter in the human c-myb proto-oncogene". Oncogene. 9 (1): 227–35.
PMID8302584.
Favier D, Gonda TJ (1994). "Detection of proteins that bind to the leucine zipper motif of c-Myb". Oncogene. 9 (1): 305–11.
PMID8302594.
Glaser R, Lafuse WP, Bonneau RH, Atkinson C, Kiecolt-Glaser JK (1993). "Stress-associated modulation of proto-oncogene expression in human peripheral blood leukocytes". Behav. Neurosci. 107 (3): 525–9.
doi:
10.1037/0735-7044.107.3.525.
PMID8329139.
Vorbrueggen G, Lovrić J, Moelling K (1997). "Functional analysis of phosphorylation at serine 532 of human c-Myb by MAP kinase". Biol. Chem. 377 (11): 721–30.
doi:
10.1515/bchm3.1996.377.11.721.
PMID8960373.
The Myb gene family is named after the eponymous gene in
Avian myeloblastosis virus. The viral Myb (v-Myb, P01104) recognizes the sequence 5'-
YAAC
KG-3'. It causes myeloblastosis (myeloid leukemia) in chickens.[7] 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.[8]
Animals
Myb proto-oncogene protein is a member of the MYB (myeloblastosis) family of
transcription factors. The protein contains three domains, an
N-terminalDNA-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.[8]
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.[9]
In maize,
phlobaphenes are synthesized in the flavonoids synthetic pathway[10] from polymerisation of
flavan-4-ols[11][12] which encodes an R2R3 myb-like
transcriptional activator[13] of the A1 gene encoding for the
dihydroflavonol 4-reductase (reducing
dihydroflavonols into flavan-4-ols)[14] while another gene (Suppressor of Pericarp Pigmentation 1 or SPP1) acts as a
suppressor.[15] The maize P gene encodes a Myb homolog that recognizes the sequence CCWACC, in sharp contrast with the YAACGG bound by vertebrate Myb proteins.[16]
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.[19]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Chen Y, Xu H, Liu J, Zhang C, Leutz A, Mo X (Jul 2007). "The c-Myb functions as a downstream target of PDGF-mediated survival signal in vascular smooth muscle cells". Biochem Biophys Res Commun. 360 (2): 433–6.
doi:
10.1016/j.bbrc.2007.06.078.
PMID17599807.
^Lee EA, Harper V (2002). "Suppressor of Pericarp Pigmentation 1 (SPP1), a novel gene involved in phlobaphene accumulation in maize (Zea mays L.) pericarps". Maydica. 47 (1): 51–58.
INIST13772300
^Grotewold E, Drummond BJ, Bowen B, Peterson T (1994). "The myb-homologous P gene controls phlobaphene pigmentation in maize floral organs by directly activating a flavonoid biosynthetic gene subset". Cell. 76 (3): 543–554.
doi:
10.1016/0092-8674(94)90117-1.
PMID8313474.
S2CID42197232.
^Boddu J, Svabek C, Ibraheem F, Jones AD, Chopra S (2005). "Characterization of a deletion allele of a sorghum Myb gene yellow seedl showing loss of 3-deoxyflavonoids". Plant Science. 169 (3): 542–552.
doi:
10.1016/j.plantsci.2005.05.007.
INIST16983977
^Boddu J, Jiang C, Sangar V, Olson T, Peterson T, Chopra S (January 2006). "Comparative structural and functional characterization of sorghum and maize duplications containing orthologous myb transcription regulators of 3-deoxyflavonoid biosynthesis". Plant Mol. Biol. 60 (2): 185–99.
doi:
10.1007/s11103-005-3568-1.
PMID16429259.
S2CID23841582.
Kalkbrenner F, Guehmann S, Moelling K (1990). "Transcriptional activation by human c-myb and v-myb genes". Oncogene. 5 (5): 657–61.
PMID2189102.
Westin EH, Gorse KM, Clarke MF (1990). "Alternative splicing of the human c-myb gene". Oncogene. 5 (8): 1117–24.
PMID2202948.
Dasgupta P, Reddy EP (1990). "Identification of alternatively spliced transcripts for human c-myb: molecular cloning and sequence analysis of human c-myb exon 9A sequences". Oncogene. 4 (12): 1419–23.
PMID2687764.
Janssen JW, Vernole P, de Boer PA, Oosterhuis JW, Collard JG (1986). "Sublocalization of c-myb to 6q21----q23 by in situ hybridization and c-myb expression in a human teratocarcinoma with 6q rearrangements". Cytogenet. Cell Genet. 41 (3): 129–35.
doi:
10.1159/000132217.
PMID3007038.
Slamon DJ, Boone TC, Murdock DC, Keith DE, Press MF, Larson RA, Souza LM (1986). "Studies of the human c-myb gene and its product in human acute leukemias". Science. 233 (4761): 347–51.
Bibcode:
1986Sci...233..347S.
doi:
10.1126/science.3014652.
PMID3014652.
Krieg J, Oelgeschläger M, Janknecht R, Lüscher B (1995). "High affinity DNA binding of native full length c-Myb and differential proteolytic sensitivity of its N- and C-terminal domains". Oncogene. 10 (11): 2221–8.
PMID7784067.
Jacobs SM, Gorse KM, Westin EH (1994). "Identification of a second promoter in the human c-myb proto-oncogene". Oncogene. 9 (1): 227–35.
PMID8302584.
Favier D, Gonda TJ (1994). "Detection of proteins that bind to the leucine zipper motif of c-Myb". Oncogene. 9 (1): 305–11.
PMID8302594.
Glaser R, Lafuse WP, Bonneau RH, Atkinson C, Kiecolt-Glaser JK (1993). "Stress-associated modulation of proto-oncogene expression in human peripheral blood leukocytes". Behav. Neurosci. 107 (3): 525–9.
doi:
10.1037/0735-7044.107.3.525.
PMID8329139.
Vorbrueggen G, Lovrić J, Moelling K (1997). "Functional analysis of phosphorylation at serine 532 of human c-Myb by MAP kinase". Biol. Chem. 377 (11): 721–30.
doi:
10.1515/bchm3.1996.377.11.721.
PMID8960373.