World Library  
Flag as Inappropriate
Email this Article


Article Id: WHEBN0007076870
Reproduction Date:

Title: Myc  
Author: World Heritage Encyclopedia
Language: English
Subject: Gene duplication, Transcription factor, P14arf, MAX (gene), Oncogene
Collection: Human Proteins, Oncogenes, Transcription Factors
Publisher: World Heritage Encyclopedia


V-myc avian myelocytomatosis viral oncogene homolog
Structure of the c-Myc (red) in complex with Max (blue) and DNA (PDB 1nkp). Both proteins are binding the major groove of the DNA by forming a fork-like structure.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; MRTL; MYCC; bHLHe39; c-Myc
External IDs ChEMBL: GeneCards:
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Myc (c-Myc) is a regulator gene that codes for a transcription factor. The protein encoded by this gene is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation.[1]

A mutated version of Myc is found in many cancers, which causes Myc to be constitutively (persistently) expressed. This leads to the unregulated expression of many genes, some of which are involved in cell proliferation, and results in the formation of cancer.[1] A common human translocation involving Myc is critical to the development of most cases of Burkitt Lymphoma.[2] Malfunctions in Myc have also been found 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, 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) and recruiting histone acetyltransferases (HATs). This means that in addition to its role as a classical transcription factor, Myc also functions to regulate global chromatin structure by regulating histone acetylation both in gene-rich regions and at sites far from any known gene.[5]


  • Discovery 1
  • Structure 2
  • Function 3
  • Myc-nick 4
  • Clinical significance 5
  • Animal Models 6
  • Interactions 7
  • See also 8
  • References 9
  • Further reading 10
  • External links 11


Myc gene was first discovered in Burkitt lymphoma patients. In Burkitt lymphoma, cancer cells show chromosomal translocations, in which Chromosome 8 is frequently involved. Cloning the break-point of the fusion chromosomes revealed a gene that was similar to myelocytomatosis viral oncogene (v-Myc). Thus, the newfound cellular gene was named c-Myc.


Myc protein belongs to Myc family of transcription factors, which also includes N-Myc and L-Myc genes. Myc family of transcription factors contain bHLH/LZ (basic Helix-Loop-Helix Leucine Zipper) domain. Myc protein, through its bHLH structural motif can bind to DNA, while the leucine zipper domain allows the dimerization with its partner 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.


Myc protein is a transcription factor that activates expression of many genes through binding enhancer box sequences (E-boxes) and recruiting histone acetyltransferases (HATs). 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.[6]

Myc is activated upon various mitogenic signals such as Wnt, Shh and EGF (via the MAPK/ERK pathway). 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. Myc is a very strong proto-oncogene and it is very often found to be upregulated in many types of cancers. Myc overexpression stimulates gene amplification,[7] presumably through DNA over-replication.

There have been several studies that have clearly indicated Myc's role in cell competition.[8]

A major effect of Myc is B cell proliferation.[9]

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


Myc-nick is a cytoplasmic form of Myc produced by a partial proteolytic cleavage of full-length c-Myc and N-Myc.[10] 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 whose expression is already significantly upregulated in the absence of Myc are strongly boosted in the presence of Myc, whereas genes whose expression is low in the absence Myc get only a small boost when Myc is present.[11]

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.[12]

Amplification of the MYC gene was found in a significant number of epithelial ovarian cancer cases.[13] In TCGA datasets, the amplification of Myc occurs in several cancer types, including breast, colorectal, pancreatic, gastric, and uterine cancers.[14]

In the experimental transformation process of normal cells into cancer cells, the MYC gene can cooperate with the RAS gene.[15][16]

Expression of Myc is highly dependent on BRD4 function in some cancers.[17][18] BET inhibitors have been used to successfully block Myc function in pre-clinical cancer models and are currently being evaluated in clinical trials.[19][20]

Animal Models

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.


Myc has been shown to interact with:

Overview of signal transduction pathways involved in apoptosis.

See also



  1. ^ a b c "Myc". NCBI. 
  2. ^ Finver SN, Nishikura K, Finger LR, Haluska FG, Finan J, Nowell PC, Croce CM (May 1988). "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". Proceedings of the National Academy of Sciences of the United States of America 85 (9): 3052–6.  
  3. ^ Begley S (2013-01-09). "DNA pioneer James Watson takes aim at cancer establishments". Reuters. 
  4. ^ Gearhart J, Pashos EE, Prasad MK (2007). "Pluripotency redux--advances in stem-cell research". N. Engl. J. Med. 357 (15): 1469–72.  
  5. ^ Cotterman R, Jin VX, Krig SR, Lemen JM, Wey A, Farnham PJ, Knoepfler PS (2008). "N-Myc regulates a widespread euchromatic program in the human genome partially independent of its role as a classical transcription factor". Cancer Res. 68 (23): 9654–62.  
  6. ^ Dominguez-Sola D, Ying CY, Grandori C, Ruggiero L, Chen B, Li M, Galloway DA, Gu W, Gautier J, Dalla-Favera R (July 2007). "Non-transcriptional control of DNA replication by c-Myc". Nature 448 (7152): 445–51.  
  7. ^ Denis N, Kitzis A, Kruh J, Dautry F, Corcos D (August 1991). "Stimulation of methotrexate resistance and dihydrofolate reductase gene amplification by c-myc". Oncogene 6 (8): 1453–7.  
  8. ^ Clavería C, Giovinazzo G, Sierra R, Torres M (August 2013). "Myc-driven endogenous cell competition in the early mammalian embryo". Nature 500 (7460): 39–44.  
  9. ^ de Alboran IM, O'Hagan RC, Gärtner F, Malynn B, Davidson L, Rickert R, Rajewsky K, DePinho RA, Alt FW (January 2001). "Analysis of C-MYC function in normal cells via conditional gene-targeted mutation". Immunity 14 (1): 45–55.  
  10. ^ Conacci-Sorrell M, Ngouenet C, Eisenman RN (2010). "Myc-nick: a cytoplasmic cleavage product of Myc that promotes alpha-tubulin acetylation and cell differentiation". Cell 142 (3): 480–93.  
  11. ^ Nie Z, Hu G, Wei G, Cui K, Yamane A, Resch W, Wang R, Green DR, Tessarollo L, Casellas R, Zhao K, Levens D (September 2012). "c-Myc is a universal amplifier of expressed genes in lymphocytes and embryonic stem cells". Cell 151 (1): 68–79.  
  12. ^ Kessler JD, Kahle KT, Sun T, Meerbrey KL, Schlabach MR, Schmitt EM, Skinner SO, Xu Q, Li MZ, Hartman ZC, Rao M, Yu P, Dominguez-Vidana R, Liang AC, Solimini NL, Bernardi RJ, Yu B, Hsu T, Golding I, Luo J, Osborne CK, Creighton CJ, Hilsenbeck SG, Schiff R, Shaw CA, Elledge SJ, Westbrook TF (January 2012). "A SUMOylation-dependent transcriptional subprogram is required for Myc-driven tumorigenesis". Science 335 (6066): 348–53.  
  13. ^ Ross JS, Ali SM, Wang K, Palmer G, Yelensky R, Lipson D, Miller VA, Zajchowski D, Shawver LK, Stephens PJ (September 2013). "Comprehensive genomic profiling of epithelial ovarian cancer by next generation sequencing-based diagnostic assay reveals new routes to targeted therapies". Gynecol. Oncol. 130 (3): 554–9.  
  14. ^ Chen Y, McGee J, Chen X, Doman TN, Gong X, Zhang Y, Hamm N, Ma X, Higgs RE, Bhagwat SV, Buchanan S, Peng SB, Staschke KA, Yadav V, Yue Y, Kouros-Mehr H (2014). "Identification of druggable cancer driver genes amplified across TCGA datasets". PLoS ONE 9 (5): e98293.  
  15. ^ Land H, Parada LF, Weinberg RA (1983). "Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes". Nature 304 (5927): 596–602.  
  16. ^ Radner H, el-Shabrawi Y, Eibl RH, Brüstle O, Kenner L, Kleihues P, Wiestler OD (1993). "Tumor induction by ras and myc oncogenes in fetal and neonatal brain: modulating effects of developmental stage and retroviral dose". Acta Neuropathol. 86 (5): 456–65.  
  17. ^ Fowler T, Ghatak P, Price DH, Conaway R, Conaway J, Chiang CM, Bradner JE, Shilatifard A, Roy AL (2014). "Regulation of MYC expression and differential JQ1 sensitivity in cancer cells". PloS One 9 (1): e87003.  
  18. ^ Shi J, Vakoc CR (Jun 2014). "The mechanisms behind the therapeutic activity of BET bromodomain inhibition". Molecular Cell 54 (5): 728–36.  
  19. ^ Delmore JE, Issa GC, Lemieux ME, Rahl PB, Shi J, Jacobs HM, Kastritis E, Gilpatrick T, Paranal RM, Qi J, Chesi M, Schinzel AC, McKeown MR, Heffernan TP, Vakoc CR, Bergsagel PL, Ghobrial IM, Richardson PG, Young RA, Hahn WC, Anderson KC, Kung AL, Bradner JE, Mitsiades CS (Sep 2011). "BET bromodomain inhibition as a therapeutic strategy to target c-Myc". Cell 146 (6): 904–17.  
  20. ^ Fu LL, Tian M, Li X, Li JJ, Huang J, Ouyang L, Zhang Y, Liu B (Mar 2015). "Inhibition of BET bromodomains as a therapeutic strategy for cancer drug discovery". Oncotarget 6 (8): 5501–16.  
  21. ^ a b c d Park J, Wood MA, Cole MD (2002). "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation". Mol. Cell. Biol. 22 (5): 1307–16.  
  22. ^ a b Li H, Lee TH, Avraham H (2002). "A novel tricomplex of BRCA1, Nmi, and c-Myc inhibits c-Myc-induced human telomerase reverse transcriptase gene (hTERT) promoter activity in breast cancer". J. Biol. Chem. 277 (23): 20965–73.  
  23. ^ Xiong J, Fan S, Meng Q, Schramm L, Wang C, Bouzahza B, Zhou J, Zafonte B, Goldberg ID, Haddad BR, Pestell RG, Rosen EM (2003). "BRCA1 inhibition of telomerase activity in cultured cells". Mol. Cell. Biol. 23 (23): 8668–90.  
  24. ^ Zhou C, Liu J (2003). "Inhibition of human telomerase reverse transcriptase gene expression by BRCA1 in human ovarian cancer cells". Biochem. Biophys. Res. Commun. 303 (1): 130–6.  
  25. ^ Wang Q, Zhang H, Kajino K, Greene MI (1998). "BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells". Oncogene 17 (15): 1939–48.  
  26. ^ a b Jin Z, Gao F, Flagg T, Deng X (2004). "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". J. Biol. Chem. 279 (38): 40209–19.  
  27. ^ Kanazawa S, Soucek L, Evan G, Okamoto T, Peterlin BM (2003). "c-Myc recruits P-TEFb for transcription, cellular proliferation and apoptosis". Oncogene 22 (36): 5707–11.  
  28. ^ Dingar D, Kalkat M, Chan P, Srikumar T, Bailey SD, Tu WB, Coyaud E, Ponzielli R, Kolyar, M, Jurisica I, Huang A, Lupien M, Penn LZ, Raught, B (2014). "BioID identifies novel c-MYC interacting partners in cultured cells and xenograft tumors.". J. Proteomics 118 (8): 95–111.  
  29. ^ Brenner C, Deplus R, Didelot C, Loriot A, Viré E, De Smet C, Gutierrez A, Danovi D, Bernard D, Boon T, Pelicci PG, Amati B, Kouzarides T, de Launoit Y, Di Croce L, Fuks F (2005). "Myc represses transcription through recruitment of DNA methyltransferase corepressor". EMBO J. 24 (2): 336–46.  
  30. ^ a b Fuchs M, Gerber J, Drapkin R, Sif S, Ikura T, Ogryzko V, Lane WS, Nakatani Y, Livingston DM (2001). "The p400 complex is an essential E1A transformation target". Cell 106 (3): 297–307.  
  31. ^ Roy AL, Carruthers C, Gutjahr T, Roeder RG (1993). "Direct role for Myc in transcription initiation mediated by interactions with TFII-I". Nature 365 (6444): 359–61.  
  32. ^ Frank SR, Parisi T, Taubert S, Fernandez P, Fuchs M, Chan HM, Livingston DM, Amati B (2003). "MYC recruits the TIP60 histone acetyltransferase complex to chromatin". EMBO Rep. 4 (6): 575–80.  
  33. ^ Chang TC, Yu D, Lee YS, Wentzel EA, Arking DE, West KM, Dang CV, Thomas-Tikhonenko A, Mendell JT (2008). "Widespread microRNA repression by Myc contributes to tumorigenesis". Nat. Genet. 40 (1): 43–50.  
  34. ^ Koscianska E, Baev V, Skreka K, Oikonomaki K, Rusinov V, Tabler M, Kalantidis K (2007). "Prediction and preliminary validation of oncogene regulation by miRNAs". BMC Mol. Biol. 8: 79.  
  35. ^ Ioannidis P, Mahaira LG, Perez SA, Gritzapis AD, Sotiropoulou PA, Kavalakis GJ, Antsaklis AI, Baxevanis CN, Papamichail M (2005). "CRD-BP/IMP1 expression characterizes cord blood CD34+ stem cells and affects c-myc and IGF-II expression in MCF-7 cancer cells". J. Biol. Chem. 280 (20): 20086–93.  
  36. ^ Gupta S, Davis RJ (1994). "MAP kinase binds to the NH2-terminal activation domain of c-Myc". FEBS Lett. 353 (3): 281–5.  
  37. ^ Tournier C, Whitmarsh AJ, Cavanagh J, Barrett T, Davis RJ (1997). "Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase". Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7337–42.  
  38. ^ Noguchi K, Kitanaka C, Yamana H, Kokubu A, Mochizuki T, Kuchino Y (1999). "Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase". J. Biol. Chem. 274 (46): 32580–7.  
  39. ^ a b 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89.  
  40. ^ a b McMahon SB, Wood MA, Cole MD (2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc". Mol. Cell. Biol. 20 (2): 556–62.  
  41. ^ a b McMahon SB, Van Buskirk HA, Dugan KA, Copeland TD, Cole MD (1998). "The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins". Cell 94 (3): 363–74.  
  42. ^ a b Cheng SW, Davies KP, Yung E, Beltran RJ, Yu J, Kalpana GV (1999). "c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function". Nat. Genet. 22 (1): 102–5.  
  43. ^ a b Mac Partlin M, Homer E, Robinson H, McCormick CJ, Crouch DH, Durant ST, Matheson EC, Hall AG, Gillespie DA, Brown R (2003). "Interactions of the DNA mismatch repair proteins MLH1 and MSH2 with c-MYC and MAX". Oncogene 22 (6): 819–25.  
  44. ^ Blackwood EM, Eisenman RN (1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science 251 (4998): 1211–7.  
  45. ^ Lee CM, Onésime D, Reddy CD, Dhanasekaran N, Reddy EP (2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". Proc. Natl. Acad. Sci. U.S.A. 99 (22): 14189–94.  
  46. ^ Billin AN, Eilers AL, Queva C, Ayer DE (1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". J. Biol. Chem. 274 (51): 36344–50.  
  47. ^ Gupta K, Anand G, Yin X, Grove L, Prochownik EV (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene 16 (9): 1149–59.  
  48. ^ 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 (1997). "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". EMBO J. 16 (10): 2892–906.  
  49. ^ Nair SK, Burley SK (2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell 112 (2): 193–205.  
  50. ^ FitzGerald MJ, Arsura M, Bellas RE, Yang W, Wu M, Chin L, Mann KK, DePinho RA, Sonenshein GE (1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene 18 (15): 2489–98.  
  51. ^ Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A (2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene 19 (29): 3266–77.  
  52. ^ Guo Q, Xie J, Dang CV, Liu ET, Bishop JM (1998). "Identification of a large Myc-binding protein that contains RCC1-like repeats". Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9172–7.  
  53. ^ Taira T, Maëda J, Onishi T, Kitaura H, Yoshida S, Kato H, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H (1998). "AMY-1, a novel C-MYC binding protein that stimulates transcription activity of C-MYC". Genes Cells 3 (8): 549–65.  
  54. ^ Izumi H, Molander C, Penn LZ, Ishisaki A, Kohno K, Funa K (2001). "Mechanism for the transcriptional repression by c-Myc on PDGF beta-receptor". J. Cell. Sci. 114 (Pt 8): 1533–44.  
  55. ^ Taira T, Sawai M, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H (1999). "Cell cycle-dependent switch of up-and down-regulation of human hsp70 gene expression by interaction between c-Myc and CBF/NF-Y". J. Biol. Chem. 274 (34): 24270–9.  
  56. ^ Uramoto H, Izumi H, Ise T, Tada M, Uchiumi T, Kuwano M, Yasumoto K, Funa K, Kohno K (2002). "p73 Interacts with c-Myc to regulate Y-box-binding protein-1 expression". J. Biol. Chem. 277 (35): 31694–702.  
  57. ^ a b c d e f Liu X, Tesfai J, Evrard YA, Dent SY, Martinez E (2003). "c-Myc transformation domain recruits the human STAGA complex and requires TRRAP and GCN5 acetylase activity for transcription activation". J. Biol. Chem. 278 (22): 20405–12.  
  58. ^ Mori K, Maeda Y, Kitaura H, Taira T, Iguchi-Ariga SM, Ariga H (1998). "MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc". J. Biol. Chem. 273 (45): 29794–800.  
  59. ^ Fujioka Y, Taira T, Maeda Y, Tanaka S, Nishihara H, Iguchi-Ariga SM, Nagashima K, Ariga H (2001). "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer". J. Biol. Chem. 276 (48): 45137–44.  
  60. ^ a b Feng XH, Liang YY, Liang M, Zhai W, Lin X (2002). "Direct interaction of c-Myc with Smad2 and Smad3 to inhibit TGF-beta-mediated induction of the CDK inhibitor p15(Ink4B)". Mol. Cell 9 (1): 133–43.  
  61. ^ Otsuki Y, Tanaka M, Kamo T, Kitanaka C, Kuchino Y, Sugimura H (2003). "Guanine nucleotide exchange factor, Tiam1, directly binds to c-Myc and interferes with c-Myc-mediated apoptosis in rat-1 fibroblasts". J. Biol. Chem. 278 (7): 5132–40.  
  62. ^ Gaubatz S, Imhof A, Dosch R, Werner O, Mitchell P, Buettner R, Eilers M (1995). "Transcriptional activation by Myc is under negative control by the transcription factor AP-2". EMBO J. 14 (7): 1508–19.  
  63. ^ 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 (Mar 2015). "Interaction with WDR5 Promotes Target Gene Recognition and Tumorigenesis by MYC". Molecular Cell 58: 1–13.  
  64. ^ Shrivastava A, Saleque S, Kalpana GV, Artandi S, Goff SP, Calame K (1993). "Inhibition of transcriptional regulator Yin-Yang-1 by association with c-Myc". Science 262 (5141): 1889–92.  
  65. ^ Staller P, Peukert K, Kiermaier A, Seoane J, Lukas J, Karsunky H, Möröy T, Bartek J, Massagué J, Hänel F, Eilers M (2001). "Repression of p15INK4b expression by Myc through association with Miz-1". Nat. Cell Biol. 3 (4): 392–9.  
  66. ^ Peukert K, Staller P, Schneider A, Carmichael G, Hänel F, Eilers M (1997). "An alternative pathway for gene regulation by Myc". EMBO J. 16 (18): 5672–86.  

Further reading

  • Ruf IK, Rhyne PW, Yang H, Borza CM, Hutt-Fletcher LM, Cleveland JL, Sample JT (2001). "EBV regulates c-MYC, apoptosis, and tumorigenicity in Burkitt's lymphoma". Curr. Top. Microbiol. Immunol. 258: 153–60.  
  • Lüscher B (2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network". Gene 277 (1-2): 1–14.  
  • Hoffman B, Amanullah A, Shafarenko M, Liebermann DA (2002). "The proto-oncogene c-myc in hematopoietic development and leukemogenesis". Oncogene 21 (21): 3414–21.  
  • Pelengaris S, Khan M, Evan G (2002). "c-MYC: more than just a matter of life and death". Nat. Rev. Cancer 2 (10): 764–76.  
  • Nilsson JA, Cleveland JL (2003). "Myc pathways provoking cell suicide and cancer". Oncogene 22 (56): 9007–21.  
  • Dang CV, O'donnell KA, Juopperi T (2005). "The great MYC escape in tumorigenesis". Cancer Cell 8 (3): 177–8.  
  • Dang CV, Li F, Lee LA (2005). "Could MYC induction of mitochondrial biogenesis be linked to ROS production and genomic instability?". Cell Cycle 4 (11): 1465–6.  
  • Coller HA, Forman JJ, Legesse-Miller A (2007). Myc'ed messages": myc induces transcription of E2F1 while inhibiting its translation via a microRNA polycistron""". PLoS Genet. 3 (8): e146.  
  • Astrin SM, Laurence J (1992). "Human immunodeficiency virus activates c-myc and Epstein-Barr virus in human B lymphocytes". Ann. N. Y. Acad. Sci. 651: 422–32.  
  • Bernstein PL, Herrick DJ, Prokipcak RD, Ross J (1992). "Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant". Genes Dev. 6 (4): 642–54.  
  • Iijima S, Teraoka H, Date T, Tsukada K (1992). "DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein". Eur. J. Biochem. 206 (2): 595–603.  
  • Seth A, Alvarez E, Gupta S, Davis RJ (1991). "A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression". J. Biol. Chem. 266 (35): 23521–4.  
  • Takahashi E, Hori T, O'Connell P, Leppert M, White R (1991). "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". Cytogenet. Cell Genet. 57 (2-3): 109–11.  
  • Blackwood EM, Eisenman RN (1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science 251 (4998): 1211–7.  
  • Gazin C, Rigolet M, Briand JP, Van Regenmortel MH, Galibert F (1986). "Immunochemical detection of proteins related to the human c-myc exon 1". EMBO J. 5 (9): 2241–50.  
  • Lüscher B, Kuenzel EA, Krebs EG, Eisenman RN (1989). "Myc oncoproteins are phosphorylated by casein kinase II". EMBO J. 8 (4): 1111–9.  
  • Finver SN, Nishikura K, Finger LR, Haluska FG, Finan J, Nowell PC, Croce CM (1988). "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". Proc. Natl. Acad. Sci. U.S.A. 85 (9): 3052–6.  
  • Showe LC, Moore RC, Erikson J, Croce CM (1987). "MYC oncogene involved in a t(8;22) chromosome translocation is not altered in its putative regulatory regions". Proc. Natl. Acad. Sci. U.S.A. 84 (9): 2824–8.  
  • Guilhot S, Petridou B, Syed-Hussain S, Galibert F (1988). "Nucleotide sequence 3' to the human c-myc oncogene; presence of a long inverted repeat". Gene 72 (1-2): 105–8.  
  • Hann SR, King MW, Bentley DL, Anderson CW, Eisenman RN (1988). "A non-AUG translational initiation in c-myc exon 1 generates an N-terminally distinct protein whose synthesis is disrupted in Burkitt's lymphomas". Cell 52 (2): 185–95.  

External links

  • The Myc Protein
  • NCBI Human Myc protein
  • Myc cancer gene
  • myc Proto-Oncogene Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
  • Generating iPS Cells from MEFS through Forced Expression of Sox-2, Oct-4, c-Myc, and Klf4
  • Myc - The Interactive FlyDrosophila
  • FactorBook C-Myc
This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from World eBook Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.