Myc
MYC proto-oncogene, bHLH transcription factor | |||||||
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Identifiers | |||||||
Symbol | MYC | ||||||
Alt. symbols | c-Myc, v-myc | ||||||
NCBI gene | 4609 | ||||||
HGNC | 7553 | ||||||
OMIM | 190080 | ||||||
RefSeq | NM_001354870.1 | ||||||
UniProt | P01106 | ||||||
Other data | |||||||
Locus | Chr. 8 q24.21 | ||||||
Wikidata | Q20969939 | ||||||
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MYCL proto-oncogene, bHLH transcription factor | |||||||
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Identifiers | |||||||
Symbol | MYCL | ||||||
Alt. symbols | LMYC, MYCL1, bHLHe38, L-Myc, v-myc | ||||||
NCBI gene | 4610 | ||||||
HGNC | 7555 | ||||||
OMIM | 164850 | ||||||
RefSeq | NM_005376 | ||||||
UniProt | P12524 | ||||||
Other data | |||||||
Locus | Chr. 1 p34.2 | ||||||
Wikidata | Q18029714 | ||||||
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MYCN proto-oncogene, bHLH transcription factor | |||||||
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Identifiers | |||||||
Symbol | MYCN | ||||||
NCBI gene | 4613 | ||||||
HGNC | 7559 | ||||||
OMIM | 164840 | ||||||
RefSeq | NM_005378 | ||||||
UniProt | V | ||||||
Other data | |||||||
Locus | Chr. 2 p24.3 | ||||||
Wikidata | Q14906753 | ||||||
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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 (MYC), l-myc (MYCL), and n-myc (MYCN). 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] Unfortunately, Myc possesses several features that have rendered it difficult to drug to date, such that any anti-cancer drugs aimed at inhibiting Myc may continue to require perturbing the protein indirectly, such as by targeting the mRNA for the protein rather than via a small molecule that targets the protein itself.[4][5]
c-Myc also plays an important role in stem cell biology and was one of the original Yamanaka factors used to reprogram somatic cells into induced pluripotent stem cells.[6]
In the human genome, C-myc is located on chromosome 8 and is believed to regulate expression of 15% of all genes[7] through binding on enhancer box sequences (E-boxes).
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.[8]
Discovery
[edit]The Myc family was first established after discovery of homology between an oncogene carried by the Avian virus, Myelocytomatosis (v-myc; P10395) and a human gene over-expressed in various cancers, cellular Myc (c-Myc).[citation needed] Later, discovery of further homologous genes in humans led to the addition of n-Myc and l-Myc to the family of genes.[9]
The most frequently discussed example of c-Myc as a proto-oncogene is its implication in Burkitt's lymphoma. In Burkitt's 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
[edit]The protein products 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
[edit]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 transcriptional elongation factors.[10] 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.[11] This activity could contribute to DNA amplification in cancer cells.[12]
Myc is activated upon various mitogenic signals such as serum stimulation or by Wnt, Shh and EGF (via the MAPK/ERK pathway).[13] 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,[14] which are necessary for Myc induced proliferation[15] or cell growth.[16]
There have been several studies that have clearly indicated Myc's role in cell competition.[17]
A major effect of c-myc is B cell proliferation, and gain of MYC has been associated with B cell malignancies and their increased aggressiveness, including histological transformation.[18] In B cells, Myc acts as a classical oncogene by regulating a number of pro-proliferative and anti-apoptotic pathways, this also includes tuning of BCR signaling and CD40 signaling in regulation of microRNAs (miR-29, miR-150, miR-17-92).[19]
c-Myc induces MTDH(AEG-1) gene expression and in turn itself requires AEG-1 oncogene for its expression.
Myc-nick
[edit]![](http://upload.wikimedia.org/wikipedia/commons/thumb/4/47/Myc-Nick.pdf/page1-330px-Myc-Nick.pdf.jpg)
Myc-nick is a cytoplasmic form of Myc produced by a partial proteolytic cleavage of full-length c-Myc and N-Myc.[20] 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
[edit]A large body of evidence shows that Myc genes and proteins are highly relevant for treating tumors.[9] 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.[6]
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.[21]
Amplification of the MYC gene was found in a significant number of epithelial ovarian cancer cases.[22] In TCGA datasets, the amplification of Myc occurs in several cancer types, including breast, colorectal, pancreatic, gastric, and uterine cancers.[23]
In the experimental transformation process of normal cells into cancer cells, the MYC gene can cooperate with the RAS gene.[24][25]
Expression of Myc is highly dependent on BRD4 function in some cancers.[26][27] BET inhibitors have been used to successfully block Myc function in pre-clinical cancer models and are currently being evaluated in clinical trials.[28]
MYC expression is controlled by a wide variety of noncoding RNAs, including miRNA, lncRNA, and circRNA. Some of these RNAs have been shown to be specific for certain types of human tissues and tumors.[29] Changes in the expression of such RNAs can potentially be used to develop targeted tumor therapy.
Animal models
[edit]In Drosophila Myc is encoded by the diminutive locus, (which was known to geneticists prior to 1935).[30] Classical diminutive alleles resulted in a viable animal with small body size. Drosophila has subsequently been used to implicate Myc in cell competition,[31] endoreplication,[32] and cell growth.[33]
During the discovery of Myc gene, it was realized that chromosomes that reciprocally translocate to chromosome 8 contained immunoglobulin genes at the break-point. 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.[34][35]
Relationship to stem cells
[edit]Myc genes play a number of normal roles in stem cells including pluripotent stem cells. In neural stem cells, N-Myc promotes a rapidly proliferative stem cell and precursor-like state in the developing brain, while inhibiting differentiation.[36] In hematopoietic stem cells, Myc controls the balance between self-renewal and differentiation.[37] In particular, long-term hematopoietic stem cells (LT-HSCs) express low levels of c-Myc, ensuring self-renewal. Enforced expression of c-Myc in LT-HSCs promotes differentiation at the expense of self-renewal, resulting in stem cell exhaustion.[38] In pathological states and specifically in acute myeloid leukemia, oxidant stress can trigger higher levels of Myc expression that affects the behavior of leukemia stem cells.[39]
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.[40]
Interactions
[edit]Myc has been shown to interact with:
- ACTL6A[41]
- BRCA1[42][43][44][45]
- Bcl-2[46]
- Cyclin T1[47]
- CHD8[48]
- DNMT3A[49]
- EP400[50]
- GTF2I[51]
- HTATIP[52]
- let-7[53][54][55]
- MAPK1[46][56][57]
- MAPK8[58]
- MAX[59][60][61][62][63][64][65][66][67][68][69][70][71]
- MLH1[63]
- MYCBP2[72]
- MYCBP[73]
- NMI[42]
- NFYB[74]
- NFYC[75]
- P73[76]
- PCAF[77]
- PFDN5[78][79]
- RuvB-like 1[41][50]
- SAP130[77]
- SMAD2[80]
- SMAD3[80]
- SMARCA4[41][59]
- SMARCB1[62]
- SUPT3H[77]
- TIAM1[81]
- TADA2L[77]
- TAF9[77]
- TFAP2A[82]
- TRRAP[41][60][61][77]
- WDR5[83]
- YY1[84] and
- ZBTB17.[85][86]
- C2orf16[87]
![](http://upload.wikimedia.org/wikipedia/commons/thumb/b/b0/Signal_transduction_pathways.svg/300px-Signal_transduction_pathways.svg.png)
See also
[edit]References
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- ^ Blackwood EM, Eisenman RN (March 1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science. 251 (4998): 1211–7. Bibcode:1991Sci...251.1211B. doi:10.1126/science.2006410. PMID 2006410.
- ^ Lee CM, Onésime D, Reddy CD, Dhanasekaran N, Reddy EP (October 2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". Proceedings of the National Academy of Sciences of the United States of America. 99 (22): 14189–94. Bibcode:2002PNAS...9914189L. doi:10.1073/pnas.232310199. PMC 137859. PMID 12391307.
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Further reading
[edit]- 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". Epstein-Barr Virus and Human Cancer. Current Topics in Microbiology and Immunology. Vol. 258. pp. 153–60. doi:10.1007/978-3-642-56515-1_10. ISBN 978-3-642-62568-8. PMID 11443860.
- Lüscher B (October 2001). "Function and regulation of the transcription factors of the Myc/Max/Mad network". Gene. 277 (1–2): 1–14. doi:10.1016/S0378-1119(01)00697-7. PMID 11602341.
- Hoffman B, Amanullah A, Shafarenko M, Liebermann DA (May 2002). "The proto-oncogene c-myc in hematopoietic development and leukemogenesis". Oncogene. 21 (21): 3414–21. doi:10.1038/sj.onc.1205400. PMID 12032779. S2CID 8720539.
- Pelengaris S, Khan M, Evan G (October 2002). "c-MYC: more than just a matter of life and death". Nature Reviews. Cancer. 2 (10): 764–76. doi:10.1038/nrc904. PMID 12360279. S2CID 13226062.
- Nilsson JA, Cleveland JL (December 2003). "Myc pathways provoking cell suicide and cancer". Oncogene. 22 (56): 9007–21. doi:10.1038/sj.onc.1207261. PMID 14663479. S2CID 24758874.
- Dang CV, O'donnell KA, Juopperi T (September 2005). "The great MYC escape in tumorigenesis". Cancer Cell. 8 (3): 177–8. doi:10.1016/j.ccr.2005.08.005. PMID 16169462.
- Dang CV, Li F, Lee LA (November 2005). "Could MYC induction of mitochondrial biogenesis be linked to ROS production and genomic instability?". Cell Cycle. 4 (11): 1465–6. doi:10.4161/cc.4.11.2121. PMID 16205115.
- Coller HA, Forman JJ, Legesse-Miller A (August 2007). ""Myc'ed messages": myc induces transcription of E2F1 while inhibiting its translation via a microRNA polycistron". PLOS Genetics. 3 (8): e146. doi:10.1371/journal.pgen.0030146. PMC 1959363. PMID 17784791.
- Astrin SM, Laurence J (May 1992). "Human immunodeficiency virus activates c-myc and Epstein-Barr virus in human B lymphocytes". Annals of the New York Academy of Sciences. 651 (1): 422–32. Bibcode:1992NYASA.651..422A. doi:10.1111/j.1749-6632.1992.tb24642.x. PMID 1318011. S2CID 31980333.
- Bernstein PL, Herrick DJ, Prokipcak RD, Ross J (April 1992). "Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant". Genes & Development. 6 (4): 642–54. doi:10.1101/gad.6.4.642. PMID 1559612.
- Iijima S, Teraoka H, Date T, Tsukada K (June 1992). "DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein". European Journal of Biochemistry. 206 (2): 595–603. doi:10.1111/j.1432-1033.1992.tb16964.x. PMID 1597196.
- Seth A, Alvarez E, Gupta S, Davis RJ (December 1991). "A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression". The Journal of Biological Chemistry. 266 (35): 23521–4. doi:10.1016/S0021-9258(18)54312-X. PMID 1748630.
- 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". Cytogenetics and Cell Genetics. 57 (2–3): 109–11. doi:10.1159/000133124. PMID 1914517.
- Blackwood EM, Eisenman RN (March 1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science. 251 (4998): 1211–7. Bibcode:1991Sci...251.1211B. doi:10.1126/science.2006410. PMID 2006410.
- Gazin C, Rigolet M, Briand JP, Van Regenmortel MH, Galibert F (September 1986). "Immunochemical detection of proteins related to the human c-myc exon 1". The EMBO Journal. 5 (9): 2241–50. doi:10.1002/j.1460-2075.1986.tb04491.x. PMC 1167107. PMID 2430795.
- Lüscher B, Kuenzel EA, Krebs EG, Eisenman RN (April 1989). "Myc oncoproteins are phosphorylated by casein kinase II". The EMBO Journal. 8 (4): 1111–9. doi:10.1002/j.1460-2075.1989.tb03481.x. PMC 400922. PMID 2663470.
- 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. Bibcode:1988PNAS...85.3052F. doi:10.1073/pnas.85.9.3052. PMC 280141. PMID 2834731.
- Showe LC, Moore RC, Erikson J, Croce CM (May 1987). "MYC oncogene involved in a t(8;22) chromosome translocation is not altered in its putative regulatory regions". Proceedings of the National Academy of Sciences of the United States of America. 84 (9): 2824–8. Bibcode:1987PNAS...84.2824S. doi:10.1073/pnas.84.9.2824. PMC 304752. PMID 3033665.
- Guilhot S, Petridou B, Syed-Hussain S, Galibert F (December 1988). "Nucleotide sequence 3' to the human c-myc oncogene; presence of a long inverted repeat". Gene. 72 (1–2): 105–8. doi:10.1016/0378-1119(88)90131-X. PMID 3243428.
- Hann SR, King MW, Bentley DL, Anderson CW, Eisenman RN (January 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. doi:10.1016/0092-8674(88)90507-7. PMID 3277717. S2CID 3012009.
External links
[edit]- InterPro signatures for protein family: IPR002418, IPR011598, IPR003327
- The Myc Protein
- NCBI Human Myc protein
- Myc cancer gene
- myc+Proto-Oncogene+Proteins at the U.S. 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 Archived 2008-04-09 at the Wayback Machine
- Drosophila Myc - The Interactive Fly
- FactorBook C-Myc
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Myc proto-oncogene protein