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词条 MAX (gene)
释义

  1. Function

  2. Interactions

  3. Clinical relevance

  4. References

  5. Further reading

  6. External links

{{Infobox_gene}}MAX (also known as myc-associated factor X) is a gene that in humans encodes the MAX transcription factor.[1][2]

Function

The protein product of MAX contains the basic helix-loop-helix and leucine zipper motifs. It is therefore included in the bHLHZ family of transcription factors. It is able to form homodimers with other MAX proteins and heterodimers with other transcription factors, including Mad, Mxl1 and Myc. The homodimers and heterodimers compete for a common DNA target site (the E-box) in a gene promoter zone. Rearrangement of dimers (e.g., Mad:Max, Max:Myc) provides a system of transcriptional regulation with greater diversity of gene targets. Max must dimerise in order to be biologically active.[3]

Transcriptionally active hetero- and homodimers involving Max can promote cell proliferation as well as apoptosis.[4]

Interactions

The protein product of Max has been shown to interact with:

  • Myc,[5][6][7][8][9][10][11][12][13][14][15][16][9]
  • MNT,[14]
  • MSH2,[10]
  • MXD1,[11][12][13][14]
  • MXI1,[15][16][17][18]
  • MYCL1,[10][17]
  • N-Myc,[19][17]
  • SPAG9,[11]
  • TEAD1,[20] and
  • Transformation/transcription domain-associated protein.[6][7]

Clinical relevance

This gene has been shown mutated in cases of hereditary pheochromocytoma.[21] More recently the Max gene becomes mutated and becomes inactivated in small cell lung cancer (SCLC). This is mutually exclusive with alterations at Myc and BRG1, the latter coding for an ATPase of the SWI/SNF complex. It was demonstrated that the BRG1 product regulates the expression of Max through direct recruitment to the Max promoter region, and that depletion of BRG1 strongly hinders cell growth, specifically in Max-deficient cells, suggesting that the two together cause synthetic lethality. Furthermore, Max required BRG1 to activate neuroendocrine transcriptional programs and to up-regulate Myc targets, such as glycolytic-related genes.[22]

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References

1. ^{{cite journal |vauthors=Wagner AJ, Le Beau MM, Diaz MO, Hay N | title = Expression, regulation, and chromosomal localization of the Max gene | journal = Proc Natl Acad Sci U S A | volume = 89 | issue = 7 | pages = 3111–5 | date = May 1992 | pmid = 1557420 | pmc = 48814 | doi = 10.1073/pnas.89.7.3111 | bibcode = 1992PNAS...89.3111W }}
2. ^{{cite web | title = Entrez Gene: MAX MYC associated factor X| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4149| accessdate = }}
3. ^{{cite journal|last1=Ecevit|first1=O|last2=Khan|first2=MA|last3=Goss|first3=DJ|title=Kinetic analysis of the interaction of b/HLH/Z transcription factors Myc, Max, and Mad with cognate DNA.|journal=Biochemistry|date=30 March 2010|volume=30|issue=42|pages=2627–2635|doi=10.1021/bi901913a|pmid=20170194|pmc=2852888}}
4. ^{{cite journal |vauthors=Amati B, Land H | title = Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death | journal = Curr. Opin. Genet. Dev. | volume = 4 | issue = 1 | pages = 102–8 | date = February 1994 | pmid = 8193530 | doi = 10.1016/0959-437X(94)90098-1 }}
5. ^{{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 = Mol. Syst. Biol. | volume = 3 | issue = | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
6. ^1 {{cite journal |vauthors=McMahon SB, Wood MA, Cole MD | title = The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc | journal = Mol. Cell. Biol. | volume = 20 | issue = 2 | pages = 556–62 | date = January 2000 | pmid = 10611234 | pmc = 85131 | doi = 10.1128/MCB.20.2.556-562.2000 }}
7. ^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 }}
8. ^{{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 = Nat. Genet. | volume = 22 | issue = 1 | pages = 102–5 | date = May 1999 | pmid = 10319872 | doi = 10.1038/8811 }}
9. ^{{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 }}
10. ^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 | url = }}
11. ^1 2 {{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 = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 22 | pages = 14189–94 | date = October 2002 | pmid = 12391307 | pmc = 137859 | doi = 10.1073/pnas.232310199 | bibcode = 2002PNAS...9914189L }}
12. ^1 {{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 }}
13. ^1 {{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 }}
14. ^{{cite journal |vauthors=Ayer DE, Kretzner L, Eisenman RN | title = Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity | journal = Cell | volume = 72 | issue = 2 | pages = 211–22 | date = January 1993 | pmid = 8425218 | doi = 10.1016/0092-8674(93)90661-9 }}
15. ^1 {{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 = J. Biol. Chem. | volume = 274 | issue = 51 | pages = 36344–50 | date = December 1999 | pmid = 10593926 | doi = 10.1074/jbc.274.51.36344 }}
16. ^1 2 {{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 = EMBO J. | volume = 16 | issue = 10 | pages = 2892–906 | date = May 1997 | pmid = 9184233 | pmc = 1169897 | doi = 10.1093/emboj/16.10.2892 }}
17. ^1 2 3 {{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 | url = }}
18. ^{{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = October 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R }}
19. ^1 2 {{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 | language = | journal = Science | volume = 251 | issue = 4998 | pages = 1211–7 | date = Mar 1991 | pmid = 2006410 | doi = 10.1126/science.2006410 | url = | laysummary = | oclc = | id = | bibcode =1991Sci...251.1211B | accessdate = | laydate = | format = | quote = | issn = 0036-8075 | laysource = }}
20. ^{{cite journal |vauthors=Gupta MP, Amin CS, Gupta M, Hay N, Zak R | title = Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression | journal = Mol. Cell. Biol. | volume = 17 | issue = 7 | pages = 3924–36 | date = July 1997 | pmid = 9199327 | pmc = 232245 | doi = 10.1128/mcb.17.7.3924}}
21. ^{{cite journal |vauthors=Comino-Méndez I, Gracia-Aznárez FJ, Schiavi F, Landa I, Leandro-García LJ, Letón R, Honrado E, Ramos-Medina R, Caronia D, Pita G, Gómez-Graña A, de Cubas AA, Inglada-Pérez L, Maliszewska A, Taschin E, Bobisse S, Pica G, Loli P, Hernández-Lavado R, Díaz JA, Gómez-Morales M, González-Neira A, Roncador G, Rodríguez-Antona C, Benítez J, Mannelli M, Opocher G, Robledo M, Cascón A | title = Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma | journal = Nat. Genet. | volume = 43 | issue = 7 | pages = 663–7 | date = July 2011 | pmid = 21685915 | doi = 10.1038/ng.861 }}
22. ^{{cite journal |vauthors=Romero OA, Torres-Diz M, Pros E, Savola S, Gomez A, Moran S, Saez C, Iwakawa R, Villanueva A, Montuenga LM, Kohno T, Yokota J, Sanchez-Cespedes M | title = MAX inactivation in small-cell lung cancer disrupts the MYC-SWI/SNF programs and is synthetic lethal with BRG1. | journal = Cancer Discov | volume = 4| issue = 3 | date = Dec 2013 | pmid = 24362264 | doi = 10.1158/2159-8290.CD-13-0799 | url = | issn = | pages=292–303}}

Further reading

{{refbegin|colwidth=35em}}
  • {{cite journal |vauthors=Grandori C, Cowley SM, James LP, Eisenman RN | title = The Myc/Max/Mad network and the transcriptional control of cell behavior. | journal = Annu. Rev. Cell Dev. Biol. | volume = 16 | issue = | pages = 653–99 | year = 2001 | pmid = 11031250 | doi = 10.1146/annurev.cellbio.16.1.653 }}
  • {{cite journal | author = 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 | year = 2001 | pmid = 11602341 | doi = 10.1016/S0378-1119(01)00697-7 }}
  • {{cite journal |vauthors=Wechsler DS, Dang CV | title = Opposite orientations of DNA bending by c-Myc and Max. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 89 | issue = 16 | pages = 7635–9 | year = 1992 | pmid = 1323849 | pmc = 49765 | doi = 10.1073/pnas.89.16.7635 | bibcode = 1992PNAS...89.7635W }}
  • {{cite journal |vauthors=Mäkelä TP, Koskinen PJ, Västrik I, Alitalo K | title = Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation. | journal = Science | volume = 256 | issue = 5055 | pages = 373–7 | year = 1992 | pmid = 1566084 | doi = 10.1126/science.256.5055.373 | bibcode = 1992Sci...256..373M }}
  • {{cite journal |vauthors=Gilladoga AD, Edelhoff S, Blackwood EM, Eisenman RN, Disteche CM | title = Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in situ hybridization. | journal = Oncogene | volume = 7 | issue = 6 | pages = 1249–51 | year = 1992 | pmid = 1594250 | doi = }}
  • {{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 | year = 1991 | pmid = 2006410 | doi = 10.1126/science.2006410 | bibcode = 1991Sci...251.1211B }}
  • {{cite journal |vauthors=Zervos AS, Faccio L, Gatto JP, Kyriakis JM, Brent R | title = Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 23 | pages = 10531–4 | year = 1995 | pmid = 7479834 | pmc = 40645 | doi = 10.1073/pnas.92.23.10531 | bibcode = 1995PNAS...9210531Z }}
  • {{cite journal |vauthors=Bousset K, Henriksson M, Lüscher-Firzlaff JM, Litchfield DW, Lüscher B | title = Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers. | journal = Oncogene | volume = 8 | issue = 12 | pages = 3211–20 | year = 1993 | pmid = 8247525 | doi = }}
  • {{cite journal |vauthors=Ayer DE, Kretzner L, Eisenman RN | title = Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. | journal = Cell | volume = 72 | issue = 2 | pages = 211–22 | year = 1993 | pmid = 8425218 | doi = 10.1016/0092-8674(93)90661-9 }}
  • {{cite journal |vauthors=Västrik I, Koskinen PJ, Alitalo R, Mäkelä TP | title = Alternative mRNA forms and open reading frames of the max gene. | journal = Oncogene | volume = 8 | issue = 2 | pages = 503–7 | year = 1993 | pmid = 8426752 | doi = }}
  • {{cite journal |vauthors=Ferré-D'Amaré AR, Prendergast GC, Ziff EB, Burley SK | title = Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. | journal = Nature | volume = 363 | issue = 6424 | pages = 38–45 | year = 1993 | pmid = 8479534 | doi = 10.1038/363038a0 | bibcode = 1993Natur.363...38F }}
  • {{cite journal |vauthors=Hurlin PJ, Quéva C, Koskinen PJ, Steingrímsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN | title = Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. | journal = EMBO J. | volume = 14 | issue = 22 | pages = 5646–59 | year = 1996 | pmid = 8521822 | pmc = 394680 | doi = 10.1002/j.1460-2075.1995.tb00252.x}}
  • {{cite journal |vauthors=Grandori C, Mac J, Siëbelt F, Ayer DE, Eisenman RN | title = Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo. | journal = EMBO J. | volume = 15 | issue = 16 | pages = 4344–57 | year = 1996 | pmid = 8861962 | pmc = 452159 | doi = 10.1002/j.1460-2075.1996.tb00808.x}}
  • {{cite journal |vauthors=Brownlie P, Ceska T, Lamers M, Romier C, Stier G, Teo H, Suck D | title = The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control. | journal = Structure | volume = 5 | issue = 4 | pages = 509–20 | year = 1997 | pmid = 9115440 | doi = 10.1016/S0969-2126(97)00207-4 }}
  • {{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 = EMBO J. | volume = 16 | issue = 10 | pages = 2892–906 | year = 1997 | pmid = 9184233 | pmc = 1169897 | doi = 10.1093/emboj/16.10.2892 }}
  • {{cite journal |vauthors=Gupta MP, Amin CS, Gupta M, Hay N, Zak R | title = Transcription enhancer factor 1 interacts with a basic helix-loop-helix zipper protein, Max, for positive regulation of cardiac alpha-myosin heavy-chain gene expression. | journal = Mol. Cell. Biol. | volume = 17 | issue = 7 | pages = 3924–36 | year = 1997 | pmid = 9199327 | pmc = 232245 | doi = 10.1128/mcb.17.7.3924}}
  • {{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 | year = 1998 | pmid = 9528857 | doi = 10.1038/sj.onc.1201634 }}
  • {{cite journal |vauthors=Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD | title = Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper. | journal = J. Mol. Biol. | volume = 281 | issue = 1 | pages = 165–81 | year = 1998 | pmid = 9680483 | doi = 10.1006/jmbi.1998.1914 }}
  • {{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 | year = 1999 | pmid = 10229200 | doi = 10.1038/sj.onc.1202611 }}
{{refend}}

External links

  • {{MeshName|MAX+protein,+human}}
  • {{FactorBook|Max}}
{{NLM content}}{{PDB Gallery|geneid=4149}}{{Transcription factors|g1}}

1 : Transcription factors
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