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词条 Myc
释义

  1. Discovery

  2. Structure

  3. Function

  4. Myc-nick

  5. Clinical significance

  6. Animal models

  7. Relationship to Stem Cells

  8. Interactions

  9. See also

  10. References

  11. Further reading

  12. External links

{{Infobox_gene}}

Myc is a family of regulator genes and proto-oncogenes that code for transcription factors. The Myc family consists of three related human genes: c-myc, l-myc, and n-myc. c-myc (also sometimes referred to as MYC) was the first gene to be discovered in this family, due to homology with the viral gene v-myc.

In cancer, c-myc is often constitutively (persistently) expressed. This leads to the increased expression of many genes, some of which are involved in cell proliferation, contributing to the formation of cancer.[1] A common human translocation involving c-myc is critical to the development of most cases of Burkitt lymphoma.[2] Constitutive upregulation of Myc genes have also been observed in carcinoma of the cervix, colon, breast, lung and stomach.[1] Myc is thus viewed as a promising target for anti-cancer drugs.[3]

In the human genome, C-myc is located on chromosome 8 and is believed to regulate expression of 15% of all genes[4] through binding on enhancer box sequences (E-boxes).[5]

In addition to its role as a classical transcription factor, N-myc may recruit histone acetyltransferases (HATs). This allows it to regulate global chromatin structure via histone acetylation.[6]

Discovery

The Myc family was first established after discovery of homology between an oncogene carried by the Avian virus, Myelocytomatosis (v-myc) and a human gene over-expressed in various cancers, cellular Myc (c-Myc). Later, discovery of further homologous genes in humans led to the addition of n-Myc and l-Myc to the family of genes.

The most frequently discussed example of c-Myc as a proto-oncogene is its implication in Burkitt lymphoma. In Burkitt lymphoma, cancer cells show chromosomal translocations, most commonly between chromosome 8 and chromosome 14 [t(8;14)]. This causes c-Myc to be placed downstream of the highly active immunoglobulin (Ig) promoter region, leading to overexpression of Myc.

Structure

The protein product of Myc family genes all belong to the Myc family of transcription factors, which contain bHLH (basic helix-loop-helix) and LZ (leucine zipper) structural motifs. The bHLH motif, allows Myc proteins to bind with DNA, while the leucine zipper TF-binding motif allows dimerization with Max, another bHLH transcription factor.

Myc mRNA contains an IRES (internal ribosome entry site) that allows the RNA to be translated into protein when 5' cap-dependent translation is inhibited, such as during viral infection.

Function

Myc proteins are transcription factors that activate expression of many pro-proliferative genes through binding enhancer box sequences (E-boxes) and recruiting histone acetyltransferases (HATs). Myc is thought to function by upregulating transcript elongation of actively transcribed genes through the recruitment of elongation factors.[7] It can also act as a transcriptional repressor. By binding Miz-1 transcription factor and displacing the p300 co-activator, it inhibits expression of Miz-1 target genes. In addition, myc has a direct role in the control of DNA replication.[8]

Myc is activated upon various mitogenic signals such as serum stimulation or by Wnt, Shh and EGF (via the MAPK/ERK pathway).[9]

By modifying the expression of its target genes, Myc activation results in numerous biological effects. The first to be discovered was its capability to drive cell proliferation (upregulates cyclins, downregulates p21), but it also plays a very important role in regulating cell growth (upregulates ribosomal RNA and proteins), apoptosis (downregulates Bcl-2), differentiation, and stem cell self-renewal. Nucleotide metabolism genes are upregulated by Myc,[10] which are necessary for Myc induced proliferation[11] or cell growth.[12]

There have been several studies that have clearly indicated Myc's role in cell competition.[13]

A major effect of c-myc is B cell proliferation.[14]

c-Myc induces MTDH(AEG-1) gene expression and in turn itself requires AEG-1 oncogene for its expression.

Myc-nick

Myc-nick is a cytoplasmic form of Myc produced by a partial proteolytic cleavage of full-length c-Myc and N-Myc.[15] Myc cleavage is mediated by the calpain family of calcium-dependent cytosolic proteases.

The cleavage of Myc by calpains is a constitutive process but is enhanced under conditions that require rapid downregulation of Myc levels, such as during terminal differentiation. Upon cleavage, the C-terminus of Myc (containing the DNA binding domain) is degraded, while Myc-nick, the N-terminal segment 298-residue segment remains in the cytoplasm. Myc-nick contains binding domains for histone acetyltransferases and for ubiquitin ligases.

The functions of Myc-nick are currently under investigation, but this new Myc family member was found to regulate cell morphology, at least in part, by interacting with acetyl transferases to promote the acetylation of α-tubulin. Ectopic expression of Myc-nick accelerates the differentiation of committed myoblasts into muscle cells.

Clinical significance

Except for early response genes, Myc universally upregulates gene expression. Furthermore, the upregulation is nonlinear. Genes for which expression is already significantly upregulated in the absence of Myc are strongly boosted in the presence of Myc, whereas genes for which expression is low in the absence Myc get only a small boost when Myc is present.[16]

Inactivation of SUMO-activating enzyme (SAE1 / SAE2) in the presence of Myc hyperactivation results in mitotic catastrophe and cell death in cancer cells. Hence inhibitors of SUMOylation may be a possible treatment for cancer.[17]

Amplification of the MYC gene was found in a significant number of epithelial ovarian cancer cases.[18] In TCGA datasets, the amplification of Myc occurs in several cancer types, including breast, colorectal, pancreatic, gastric, and uterine cancers.[19]

In the experimental transformation process of normal cells into cancer cells, the MYC gene can cooperate with the RAS gene.[20][21]

Expression of Myc is highly dependent on BRD4 function in some cancers.[22][23] BET inhibitors have been used to successfully block Myc function in pre-clinical cancer models and are currently being evaluated in clinical trials.[24][25]

Animal models

In Drosophila Myc is encoded by the diminutive locus, (which was known to geneticists prior to 1935).[26] Calssical diminutive alleles resulted in a viable animal with small body size. Drosophila has subsequently been used to implicate Myc in cell competition,[27] endoreplication,[28] and cell growth.[29]

During the discovery of Myc gene, it was realized that chromosomes that reciprocally translocate to chromosome 8 contained immunoglobulin genes at the break-point. Enhancers that normally drive expression of immunoglobin genes now lead to overexpression of Myc proto-oncogene in lymphoma cells. To study the mechanism of tumorigenesis in Burkitt lymphoma by mimicking expression pattern of Myc in these cancer cells, transgenic mouse models were developed. Myc gene placed under the control of IgM heavy chain enhancer in transgenic mice gives rise to mainly lymphomas. Later on, in order to study effects of Myc in other types of cancer, transgenic mice that overexpress Myc in different tissues (liver, breast) were also made. In all these mouse models overexpression of Myc causes tumorigenesis, illustrating the potency of Myc oncogene.

In a study with mice, reduced expression of Myc was shown to induce longevity, with significantly extended median and maximum lifespans in both sexes and a reduced mortality rate across all ages, better health, cancer progression was slower, better metabolism and they had smaller bodies. Also, Less TOR, AKT, S6K and other changes in energy and metabolic pathways (such as AMPK, more oxygen consumption, more body movements, etc.). The study by John M. Sedivy and others used Cre-Loxp -recombinase to knockout one copy of Myc and this resulted in a "Haplo-insufficient" genotype noted as Myc+/-. The phenotypes seen oppose the effects of normal aging and are shared with many other long-lived mouse models such as CR (calorie restriction) ames dwarf, rapamycin, metformin and resveratrol. One study found that Myc and p53 genes were key to the survival of Chronic Myeloid Leukaemia (CML) cells. Targeting Myc and p53 proteins with drugs gave positive results on mice with CML.[30][31]

Relationship to Stem Cells

c-Myc plays a major role in the generation of induced pluripotent stem cells (iPSCs). It is one of the original factors discovered by Yamanaka et al. to encourage cells to return to a 'stem-like' state alongside transcription factors Oct4, Sox2 and Klf4. It has since been shown that it is possible to generate iPSCs without c-Myc.

Interactions

Myc has been shown to interact with:

{{div col|colwidth=20em}}
  • ACTL6A[33]
  • BRCA1[34][32][33][34]
  • Bcl-2[35]
  • Cyclin T1[36]
  • CHD8[37]
  • DNMT3A[38]
  • EP400[42]
  • GTF2I[39]
  • HTATIP[40]
  • let-7[41][42][43]
  • MAPK1[35][44][45]
  • MAPK8[46]
  • MAX[47][48][49][50][51][52][53][54][55][56][57][58][59]
  • MLH1[51]
  • MYCBP2[60]
  • MYCBP[61]
  • NMI[62]
  • NFYB[63]
  • NFYC[64]
  • P73[65]
  • PCAF[66]
  • PFDN5[67][68]
  • RuvB-like 1[69][70]
  • SAP130[66]
  • SMAD2[78]
  • SMAD3[71]
  • SMARCA4[69][47]
  • SMARCB1[50]
  • SUPT3H[66]
  • TIAM1[72]
  • TADA2L[66]
  • TAF9[66]
  • TFAP2A[73]
  • TRRAP[69][48][49][66]
  • WDR5[74]
  • YY1[75] and
  • ZBTB17.[76][77]
{{Div col end}}{{Div col end}}

See also

  • Myc-tag
  • C-myc mRNA

References

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35. ^1 {{cite journal | vauthors = Jin Z, Gao F, Flagg T, Deng X | title = Tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone promotes functional cooperation of Bcl2 and c-Myc through phosphorylation in regulating cell survival and proliferation | journal = The Journal of Biological Chemistry | volume = 279 | issue = 38 | pages = 40209–19 | date = September 2004 | pmid = 15210690 | doi = 10.1074/jbc.M404056200 }}
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47. ^1 {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
48. ^1 {{cite journal | vauthors = McMahon SB, Wood MA, Cole MD | title = The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc | journal = Molecular and Cellular Biology | volume = 20 | issue = 2 | pages = 556–62 | date = January 2000 | pmid = 10611234 | pmc = 85131 | doi = 10.1128/mcb.20.2.556-562.2000 }}
49. ^1 {{cite journal | vauthors = McMahon SB, Van Buskirk HA, Dugan KA, Copeland TD, Cole MD | title = The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins | journal = Cell | volume = 94 | issue = 3 | pages = 363–74 | date = August 1998 | pmid = 9708738 | doi = 10.1016/s0092-8674(00)81479-8 }}
50. ^1 {{cite journal | vauthors = Cheng SW, Davies KP, Yung E, Beltran RJ, Yu J, Kalpana GV | title = c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function | journal = Nature Genetics | volume = 22 | issue = 1 | pages = 102–5 | date = May 1999 | pmid = 10319872 | doi = 10.1038/8811 }}
51. ^1 {{cite journal | vauthors = Mac Partlin M, Homer E, Robinson H, McCormick CJ, Crouch DH, Durant ST, Matheson EC, Hall AG, Gillespie DA, Brown R | title = Interactions of the DNA mismatch repair proteins MLH1 and MSH2 with c-MYC and MAX | journal = Oncogene | volume = 22 | issue = 6 | pages = 819–25 | date = February 2003 | pmid = 12584560 | doi = 10.1038/sj.onc.1206252 }}
52. ^{{cite journal | vauthors = Blackwood EM, Eisenman RN | title = Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc | journal = Science | volume = 251 | issue = 4998 | pages = 1211–7 | date = March 1991 | pmid = 2006410 | doi = 10.1126/science.2006410 }}
53. ^{{cite journal | vauthors = Lee CM, Onésime D, Reddy CD, Dhanasekaran N, Reddy EP | title = JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 22 | pages = 14189–94 | date = October 2002 | pmid = 12391307 | pmc = 137859 | doi = 10.1073/pnas.232310199 }}
54. ^{{cite journal | vauthors = Billin AN, Eilers AL, Queva C, Ayer DE | title = Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors | journal = The Journal of Biological Chemistry | volume = 274 | issue = 51 | pages = 36344–50 | date = December 1999 | pmid = 10593926 | doi = 10.1074/jbc.274.51.36344 }}
55. ^{{cite journal | vauthors = Gupta K, Anand G, Yin X, Grove L, Prochownik EV | title = Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc | journal = Oncogene | volume = 16 | issue = 9 | pages = 1149–59 | date = March 1998 | pmid = 9528857 | doi = 10.1038/sj.onc.1201634 }}
56. ^{{cite journal | vauthors = Meroni G, Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter DH, Brent R, Ballabio A, Carrozzo R | title = Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor | journal = The EMBO Journal | volume = 16 | issue = 10 | pages = 2892–906 | date = May 1997 | pmid = 9184233 | pmc = 1169897 | doi = 10.1093/emboj/16.10.2892 }}
57. ^{{cite journal | vauthors = Nair SK, Burley SK | title = X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors | journal = Cell | volume = 112 | issue = 2 | pages = 193–205 | date = January 2003 | pmid = 12553908 | doi = 10.1016/s0092-8674(02)01284-9 }}
58. ^{{cite journal | vauthors = FitzGerald MJ, Arsura M, Bellas RE, Yang W, Wu M, Chin L, Mann KK, DePinho RA, Sonenshein GE | title = Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc | journal = Oncogene | volume = 18 | issue = 15 | pages = 2489–98 | date = April 1999 | pmid = 10229200 | doi = 10.1038/sj.onc.1202611 }}
59. ^{{cite journal | vauthors = Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A | title = Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway? | journal = Oncogene | volume = 19 | issue = 29 | pages = 3266–77 | date = July 2000 | pmid = 10918583 | doi = 10.1038/sj.onc.1203634 }}
60. ^{{cite journal | vauthors = Guo Q, Xie J, Dang CV, Liu ET, Bishop JM | title = Identification of a large Myc-binding protein that contains RCC1-like repeats | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 16 | pages = 9172–7 | date = August 1998 | pmid = 9689053 | pmc = 21311 | doi = 10.1073/pnas.95.16.9172 }}
61. ^{{cite journal | vauthors = Taira T, Maëda J, Onishi T, Kitaura H, Yoshida S, Kato H, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H | title = AMY-1, a novel C-MYC binding protein that stimulates transcription activity of C-MYC | journal = Genes to Cells | volume = 3 | issue = 8 | pages = 549–65 | date = August 1998 | pmid = 9797456 | doi = 10.1046/j.1365-2443.1998.00206.x }}
62. ^1 {{cite journal | vauthors = Li H, Lee TH, Avraham H | title = A novel tricomplex of BRCA1, Nmi, and c-Myc inhibits c-Myc-induced human telomerase reverse transcriptase gene (hTERT) promoter activity in breast cancer | journal = The Journal of Biological Chemistry | volume = 277 | issue = 23 | pages = 20965–73 | date = June 2002 | pmid = 11916966 | doi = 10.1074/jbc.M112231200 }}
63. ^{{cite journal | vauthors = Izumi H, Molander C, Penn LZ, Ishisaki A, Kohno K, Funa K | title = Mechanism for the transcriptional repression by c-Myc on PDGF beta-receptor | journal = Journal of Cell Science | volume = 114 | issue = Pt 8 | pages = 1533–44 | date = April 2001 | pmid = 11282029 | doi = }}
64. ^{{cite journal | vauthors = Taira T, Sawai M, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H | title = Cell cycle-dependent switch of up-and down-regulation of human hsp70 gene expression by interaction between c-Myc and CBF/NF-Y | journal = The Journal of Biological Chemistry | volume = 274 | issue = 34 | pages = 24270–9 | date = August 1999 | pmid = 10446203 | doi = 10.1074/jbc.274.34.24270 }}
65. ^{{cite journal | vauthors = Uramoto H, Izumi H, Ise T, Tada M, Uchiumi T, Kuwano M, Yasumoto K, Funa K, Kohno K | title = p73 Interacts with c-Myc to regulate Y-box-binding protein-1 expression | journal = The Journal of Biological Chemistry | volume = 277 | issue = 35 | pages = 31694–702 | date = August 2002 | pmid = 12080043 | doi = 10.1074/jbc.M200266200 }}
66. ^1 2 3 4 5 {{cite journal | vauthors = Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E | title = c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation | journal = The Journal of Biological Chemistry | volume = 278 | issue = 22 | pages = 20405–12 | date = May 2003 | pmid = 12660246 | pmc = 4031917 | doi = 10.1074/jbc.M211795200 }}
67. ^{{cite journal | vauthors = Mori K, Maeda Y, Kitaura H, Taira T, Iguchi-Ariga SM, Ariga H | title = MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc | journal = The Journal of Biological Chemistry | volume = 273 | issue = 45 | pages = 29794–800 | date = November 1998 | pmid = 9792694 | doi = 10.1074/jbc.273.45.29794 }}
68. ^{{cite journal | vauthors = Fujioka Y, Taira T, Maeda Y, Tanaka S, Nishihara H, Iguchi-Ariga SM, Nagashima K, Ariga H | title = MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer | journal = The Journal of Biological Chemistry | volume = 276 | issue = 48 | pages = 45137–44 | date = November 2001 | pmid = 11567024 | doi = 10.1074/jbc.M106127200 }}
69. ^1 2 3 {{cite journal | vauthors = Park J, Wood MA, Cole MD | title = BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation | journal = Molecular and Cellular Biology | volume = 22 | issue = 5 | pages = 1307–16 | date = March 2002 | pmid = 11839798 | pmc = 134713 | doi = 10.1128/mcb.22.5.1307-1316.2002 }}
70. ^1 {{cite journal | vauthors = Fuchs M, Gerber J, Drapkin R, Sif S, Ikura T, Ogryzko V, Lane WS, Nakatani Y, Livingston DM | title = The p400 complex is an essential E1A transformation target | journal = Cell | volume = 106 | issue = 3 | pages = 297–307 | date = August 2001 | pmid = 11509179 | doi = 10.1016/s0092-8674(01)00450-0 }}
71. ^1 {{cite journal | vauthors = Feng XH, Liang YY, Liang M, Zhai W, Lin X | title = Direct interaction of c-Myc with Smad2 and Smad3 to inhibit TGF-beta-mediated induction of the CDK inhibitor p15(Ink4B) | journal = Molecular Cell | volume = 9 | issue = 1 | pages = 133–43 | date = January 2002 | pmid = 11804592 | doi = 10.1016/s1097-2765(01)00430-0 }}
72. ^{{cite journal | vauthors = Otsuki Y, Tanaka M, Kamo T, Kitanaka C, Kuchino Y, Sugimura H | title = Guanine nucleotide exchange factor, Tiam1, directly binds to c-Myc and interferes with c-Myc-mediated apoptosis in rat-1 fibroblasts | journal = The Journal of Biological Chemistry | volume = 278 | issue = 7 | pages = 5132–40 | date = February 2003 | pmid = 12446731 | doi = 10.1074/jbc.M206733200 }}
73. ^{{cite journal | vauthors = Gaubatz S, Imhof A, Dosch R, Werner O, Mitchell P, Buettner R, Eilers M | title = Transcriptional activation by Myc is under negative control by the transcription factor AP-2 | journal = The EMBO Journal | volume = 14 | issue = 7 | pages = 1508–19 | date = April 1995 | pmid = 7729426 | pmc = 398238 | doi = 10.1002/j.1460-2075.1995.tb07137.x}}
74. ^{{cite journal | vauthors = Thomas LR, Wang Q, Grieb BC, Phan J, Foshage AM, Sun Q, Olejniczak ET, Clark T, Dey S, Lorey S, Alicie B, Howard GC, Cawthon B, Ess KC, Eischen CM, Zhao Z, Fesik SW, Tansey WP | title = Interaction with WDR5 promotes target gene recognition and tumorigenesis by MYC | journal = Molecular Cell | volume = 58 | issue = 3 | pages = 440–52 | date = May 2015 | pmid = 25818646 | pmc = 4427524 | doi = 10.1016/j.molcel.2015.02.028 }}
75. ^{{cite journal | vauthors = Shrivastava A, Saleque S, Kalpana GV, Artandi S, Goff SP, Calame K | title = Inhibition of transcriptional regulator Yin-Yang-1 by association with c-Myc | journal = Science | volume = 262 | issue = 5141 | pages = 1889–92 | date = December 1993 | pmid = 8266081 | doi = 10.1126/science.8266081 }}
76. ^{{cite journal | vauthors = Staller P, Peukert K, Kiermaier A, Seoane J, Lukas J, Karsunky H, Möröy T, Bartek J, Massagué J, Hänel F, Eilers M | title = Repression of p15INK4b expression by Myc through association with Miz-1 | journal = Nature Cell Biology | volume = 3 | issue = 4 | pages = 392–9 | date = April 2001 | pmid = 11283613 | doi = 10.1038/35070076 }}
77. ^{{cite journal | vauthors = Peukert K, Staller P, Schneider A, Carmichael G, Hänel F, Eilers M | title = An alternative pathway for gene regulation by Myc | journal = The EMBO Journal | volume = 16 | issue = 18 | pages = 5672–86 | date = September 1997 | pmid = 9312026 | pmc = 1170199 | doi = 10.1093/emboj/16.18.5672 }}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors = Ruf IK, Rhyne PW, Yang H, Borza CM, Hutt-Fletcher LM, Cleveland JL, Sample JT | title = EBV regulates c-MYC, apoptosis, and tumorigenicity in Burkitt's lymphoma | journal = Current Topics in Microbiology and Immunology | volume = 258 | issue = | pages = 153–60 | year = 2001 | pmid = 11443860 | doi = }}
  • {{cite journal | vauthors = Lüscher B | title = Function and regulation of the transcription factors of the Myc/Max/Mad network | journal = Gene | volume = 277 | issue = 1–2 | pages = 1–14 | date = October 2001 | pmid = 11602341 | doi = 10.1016/S0378-1119(01)00697-7 }}
  • {{cite journal | vauthors = Hoffman B, Amanullah A, Shafarenko M, Liebermann DA | title = The proto-oncogene c-myc in hematopoietic development and leukemogenesis | journal = Oncogene | volume = 21 | issue = 21 | pages = 3414–21 | date = May 2002 | pmid = 12032779 | doi = 10.1038/sj.onc.1205400 }}
  • {{cite journal | vauthors = Pelengaris S, Khan M, Evan G | title = c-MYC: more than just a matter of life and death | journal = Nature Reviews. Cancer | volume = 2 | issue = 10 | pages = 764–76 | date = October 2002 | pmid = 12360279 | doi = 10.1038/nrc904 }}
  • {{cite journal | vauthors = Nilsson JA, Cleveland JL | title = Myc pathways provoking cell suicide and cancer | journal = Oncogene | volume = 22 | issue = 56 | pages = 9007–21 | date = December 2003 | pmid = 14663479 | doi = 10.1038/sj.onc.1207261 }}
  • {{cite journal | vauthors = Dang CV, O'donnell KA, Juopperi T | title = The great MYC escape in tumorigenesis | journal = Cancer Cell | volume = 8 | issue = 3 | pages = 177–8 | date = September 2005 | pmid = 16169462 | doi = 10.1016/j.ccr.2005.08.005 }}
  • {{cite journal | vauthors = Dang CV, Li F, Lee LA | title = Could MYC induction of mitochondrial biogenesis be linked to ROS production and genomic instability? | journal = Cell Cycle | volume = 4 | issue = 11 | pages = 1465–6 | date = November 2005 | pmid = 16205115 | doi = 10.4161/cc.4.11.2121 }}
  • {{cite journal | vauthors = Coller HA, Forman JJ, Legesse-Miller A | title = "Myc'ed messages": myc induces transcription of E2F1 while inhibiting its translation via a microRNA polycistron | journal = PLoS Genetics | volume = 3 | issue = 8 | pages = e146 | date = August 2007 | pmid = 17784791 | pmc = 1959363 | doi = 10.1371/journal.pgen.0030146 }}
  • {{cite journal | vauthors = Astrin SM, Laurence J | title = Human immunodeficiency virus activates c-myc and Epstein-Barr virus in human B lymphocytes | journal = Annals of the New York Academy of Sciences | volume = 651 | issue = | pages = 422–32 | date = May 1992 | pmid = 1318011 | doi = 10.1111/j.1749-6632.1992.tb24642.x }}
  • {{cite journal | vauthors = Bernstein PL, Herrick DJ, Prokipcak RD, Ross J | title = Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant | journal = Genes & Development | volume = 6 | issue = 4 | pages = 642–54 | date = April 1992 | pmid = 1559612 | doi = 10.1101/gad.6.4.642 }}
  • {{cite journal | vauthors = Iijima S, Teraoka H, Date T, Tsukada K | title = DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein | journal = European Journal of Biochemistry / FEBS | volume = 206 | issue = 2 | pages = 595–603 | date = June 1992 | pmid = 1597196 | doi = 10.1111/j.1432-1033.1992.tb16964.x }}
  • {{cite journal | vauthors = Seth A, Alvarez E, Gupta S, Davis RJ | title = A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression | journal = The Journal of Biological Chemistry | volume = 266 | issue = 35 | pages = 23521–4 | date = December 1991 | pmid = 1748630 | doi = }}
  • {{cite journal | vauthors = Takahashi E, Hori T, O'Connell P, Leppert M, White R | title = Mapping of the MYC gene to band 8q24.12----q24.13 by R-banding and distal to fra(8)(q24.11), FRA8E, by fluorescence in situ hybridization | journal = Cytogenetics and Cell Genetics | volume = 57 | issue = 2–3 | pages = 109–11 | year = 1991 | pmid = 1914517 | doi = 10.1159/000133124 }}
  • {{cite journal | vauthors = Blackwood EM, Eisenman RN | title = Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc | journal = Science | volume = 251 | issue = 4998 | pages = 1211–7 | date = March 1991 | pmid = 2006410 | doi = 10.1126/science.2006410 }}
  • {{cite journal | vauthors = Gazin C, Rigolet M, Briand JP, Van Regenmortel MH, Galibert F | title = Immunochemical detection of proteins related to the human c-myc exon 1 | journal = The EMBO Journal | volume = 5 | issue = 9 | pages = 2241–50 | date = September 1986 | pmid = 2430795 | pmc = 1167107 | doi = 10.1002/j.1460-2075.1986.tb04491.x}}
  • {{cite journal | vauthors = Lüscher B, Kuenzel EA, Krebs EG, Eisenman RN | title = Myc oncoproteins are phosphorylated by casein kinase II | journal = The EMBO Journal | volume = 8 | issue = 4 | pages = 1111–9 | date = April 1989 | pmid = 2663470 | pmc = 400922 | doi = 10.1002/j.1460-2075.1989.tb03481.x}}
  • {{cite journal | vauthors = Finver SN, Nishikura K, Finger LR, Haluska FG, Finan J, Nowell PC, Croce CM | title = Sequence analysis of the MYC oncogene involved in the t(8;14)(q24;q11) chromosome translocation in a human leukemia T-cell line indicates that putative regulatory regions are not altered | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 85 | issue = 9 | pages = 3052–6 | date = May 1988 | pmid = 2834731 | pmc = 280141 | doi = 10.1073/pnas.85.9.3052 }}
  • {{cite journal | vauthors = Showe LC, Moore RC, Erikson J, Croce CM | title = MYC oncogene involved in a t(8;22) chromosome translocation is not altered in its putative regulatory regions | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 9 | pages = 2824–8 | date = May 1987 | pmid = 3033665 | pmc = 304752 | doi = 10.1073/pnas.84.9.2824 }}
  • {{cite journal | vauthors = Guilhot S, Petridou B, Syed-Hussain S, Galibert F | title = Nucleotide sequence 3' to the human c-myc oncogene; presence of a long inverted repeat | journal = Gene | volume = 72 | issue = 1–2 | pages = 105–8 | date = December 1988 | pmid = 3243428 | doi = 10.1016/0378-1119(88)90131-X }}
  • {{cite journal | vauthors = Hann SR, King MW, Bentley DL, Anderson CW, Eisenman RN | title = A non-AUG translational initiation in c-myc exon 1 generates an N-terminally distinct protein whose synthesis is disrupted in Burkitt's lymphomas | journal = Cell | volume = 52 | issue = 2 | pages = 185–95 | date = January 1988 | pmid = 3277717 | doi = 10.1016/0092-8674(88)90507-7 }}
{{refend}}

External links

  • The Myc Protein
  • [https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=protein&val=71774083 NCBI Human Myc protein]
  • Myc cancer gene
  • {{MeshName|myc+Proto-Oncogene+Proteins}}
  • Generating iPS Cells from MEFS through Forced Expression of Sox-2, Oct-4, c-Myc, and Klf4
  • Drosophila Myc - The Interactive Fly
  • {{FactorBook|C-Myc}}
{{PDB Gallery|geneid=4609}}{{Oncogenes}}{{Transcription factors|g1}}

3 : Oncogenes|Transcription factors|Human proteins
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