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{{Infobox_gene}}
{{PBB_Controls
'''Protein max''' also known as '''myc-associated factor X''' is a [[protein]] that in humans is encoded by the ''MAX'' [[gene]].<ref name="pmid1557420">{{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 }}</ref><ref name="entrez">{{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 = }}</ref>
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| require_manual_inspection = no
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_MAX_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1an2.
| PDB = {{PDB2|1an2}}, {{PDB2|1hlo}}, {{PDB2|1nkp}}, {{PDB2|1nlw}}, {{PDB2|1r05}}
| Name = MYC associated factor X
| HGNCid = 6913
| Symbol = MAX
| AltSymbols =; MGC10775; MGC11225; MGC18164; MGC34679; MGC36767; orf1
| OMIM = 154950
| ECnumber = 
| Homologene = 1786
| MGIid = 96921
| GeneAtlas_image1 = PBB_GE_MAX_214108_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAX_208403_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_MAX_209331_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4149
    | Hs_Ensembl = ENSG00000125952
    | Hs_RefseqProtein = NP_002373
    | Hs_RefseqmRNA = NM_002382
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 64542645
    | Hs_GenLoc_end = 64638980
    | Hs_Uniprot = P61244
    | Mm_EntrezGene = 17187
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_001002021
    | Mm_RefseqProtein = XP_001002021
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''MYC associated factor X''', also known as '''MAX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAX MYC associated factor X| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4149| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein max is a member of the [[basic helix-loop-helix]] [[leucine zipper]] ([[Basic helix-loop-helix leucine zipper transcription factors|bHLHZ]]) family of [[transcription factor]]s. It is able to form homodimers and heterodimers with other family members, which include [[MXD1|Mad]], [[MXI1|Mxl1]] and [[Myc]]. Myc is an [[oncogene|oncoprotein]] implicated in [[cell growth|cell proliferation]], [[cell differentiation|differentiation]] and [[apoptosis]]. The homodimers and heterodimers compete for a common DNA target site (the [[E-box]]) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown.<ref name="entrez"/>
{{PBB_Summary
 
| section_title =
Max binds to itself and to other transcription factors through its leucine zipper to form homo- and hetero-dimers respectively. Max itself lacks a [[transactivation]] domain so that Max homodimers have a repressive function.  In contrast, Myc contains a transactivation domain but cannot homodimerize.  However Myc can heterodimerize with Max to form heterodimers that can both bind DNA and transactivate. The transcriptionally active Max/Myc dimer promotes cell proliferation as well as [[apoptosis]].<ref name="pmid8193530">{{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 }}</ref>
| summary_text = The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown.<ref name="entrez">{{cite web | title = Entrez Gene: MAX MYC associated factor X| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4149| accessdate = }}</ref>
 
}}
== Interactions ==
 
MAX (gene) has been shown to [[Protein-protein interaction|interact]] with:
*  [[Myc]],<ref name="pmid17353931">{{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 }}</ref><ref name="pmid10611234">{{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 }}</ref><ref name="pmid9708738">{{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 }}</ref><ref name="pmid10319872">{{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 }}</ref><ref name=pmid12584560/><ref name=pmid2006410/><ref name=pmid12391307/><ref name=pmid10593926/><ref name=pmid9528857/><ref name=pmid9184233/><ref name=pmid12553908/><ref name=pmid10229200/><ref name="pmid10918583">{{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 }}</ref>
* [[MNT (gene)|MNT]],<ref name=pmid9184233/>
* [[MSH2]],<ref name="pmid12584560">{{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 =  }}</ref>
* [[MXD1]],<ref name="pmid12391307">{{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 }}</ref><ref name="pmid9528857">{{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 }}</ref><ref name="pmid12553908">{{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 }}</ref><ref name="pmid8425218">{{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 }}</ref>
* [[MXI1]],<ref name="pmid10593926">{{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 }}</ref><ref name="pmid9184233">{{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 }}</ref><ref name="pmid10229200">{{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 = }}</ref><ref name="pmid16189514">{{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 }}</ref>
* [[MYCL1]],<ref name=pmid2006410/><ref name=pmid10229200/>
* [[N-Myc]],<ref name=pmid2006410>{{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 (journal)|Science]] | volume = 251 | issue = 4998 | pages = 1211–7 | date = Mar 1991 | pmid = 2006410 | doi = 10.1126/science.2006410 | url =  | laysummary =  | oclc =  | id =  | bibcode =  | accessdate =  | location = UNITED STATES | laydate =  | format =  | quote =  | publisher =  | issn = 0036-8075 | laysource =  }}</ref><ref name=pmid10229200/>
* [[SPAG9]],<ref name=pmid12391307/>
* [[TEAD1]],<ref name="pmid9199327">{{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}}</ref> and
* [[Transformation/transcription domain-associated protein]].<ref name=pmid10611234/><ref name=pmid9708738/>
 
==Clinical relevance==
This gene has been shown mutated in cases of hereditary [[pheochromocytoma]].<ref name="pmid21685915">{{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 }}</ref> More recently the MAX gene has been shown to be mutated also 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 BRG1 regulates the expression of MAX through direct recruitment to the MAX promoter, and that depletion of BRG1 strongly hinders cell growth, specifically in MAX-deficient cells, heralding a synthetic lethal interaction. Furthermore, MAX required BRG1 to activate neuroendocrine transcriptional programs and to up-regulate MYC-targets, such as glycolytic-related genes.<ref name="pmid24362264">{{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| date = Dec 2013 | pmid = 24362264 | doi = 10.1158/2159-8290.CD-13-0799 | url =  | issn = | pages=292–303}}</ref>
{{Clear}}


==References==
==References==
{{reflist|2}}
{{reflist|colwidth=35em}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin|colwidth=35em}}
{{PBB_Further_reading
*{{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 }}
| citations =
*{{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 | author=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 |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 }}
*{{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= }}
*{{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 }}
*{{cite journal | author=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 |doi= }}
*{{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 | author=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 |year= 1992 |pmid= 1557420 |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 }}
*{{cite journal | author=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=  }}
*{{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 }}
*{{cite journal | author=Gilladoga AD, Edelhoff S, Blackwood EM, ''et al.'' |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=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 | author=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= }}
*{{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 | author=Zervos AS, Faccio L, Gatto JP, ''et al.'' |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 |doi=  }}
*{{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 | author=Bousset K, Henriksson M, Lüscher-Firzlaff JM, ''et al.'' |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=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 }}
*{{cite journal | author=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=  }}
*{{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 = }}
*{{cite journal | author=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=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 =  }}
*{{cite journal | author=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 }}
*{{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 | author=Hurlin PJ, Quéva C, Koskinen PJ, ''et al.'' |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 |doi=  }}
*{{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 | author=Grandori C, Mac J, Siëbelt F, ''et al.'' |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 |doi= }}
*{{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 | author=Brownlie P, Ceska T, Lamers M, ''et al.'' |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= }}
*{{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 | author=Meroni G, Reymond A, Alcalay M, ''et al.'' |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 |doi= 10.1093/emboj/16.10.2892 }}
*{{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 | author=Gupta MP, Amin CS, Gupta M, ''et al.'' |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 |doi= }}
*{{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 }}
*{{cite journal | author=Gupta K, Anand G, Yin X, ''et al.'' |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 | author=Lavigne P, Crump MP, Gagné SM, ''et al.'' |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  | author=FitzGerald MJ, Arsura M, Bellas RE, ''et al.'' |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}}
{{refend}}


== External links ==
== External links ==
* {{MeshName|MAX+protein,+human}}
* {{MeshName|MAX+protein,+human}}
* {{FactorBook|Max}}


{{NLM content}}
{{PDB Gallery|geneid=4149}}
{{Transcription factors|g1}}


{{protein-stub}}
{{NLM content}}
{{Transcription factors}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
{{WikiDoc Sources}}

Revision as of 06:11, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Protein max also known as myc-associated factor X is a protein that in humans is encoded by the MAX gene.[1][2]

Function

The protein max is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxl1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E-box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown.[2]

Max binds to itself and to other transcription factors through its leucine zipper to form homo- and hetero-dimers respectively. Max itself lacks a transactivation domain so that Max homodimers have a repressive function. In contrast, Myc contains a transactivation domain but cannot homodimerize. However Myc can heterodimerize with Max to form heterodimers that can both bind DNA and transactivate. The transcriptionally active Max/Myc dimer promotes cell proliferation as well as apoptosis.[3]

Interactions

MAX (gene) has been shown to interact with:

Clinical relevance

This gene has been shown mutated in cases of hereditary pheochromocytoma.[20] More recently the MAX gene has been shown to be mutated also 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 BRG1 regulates the expression of MAX through direct recruitment to the MAX promoter, and that depletion of BRG1 strongly hinders cell growth, specifically in MAX-deficient cells, heralding a synthetic lethal interaction. Furthermore, MAX required BRG1 to activate neuroendocrine transcriptional programs and to up-regulate MYC-targets, such as glycolytic-related genes.[21]

References

  1. ↑ Wagner AJ, Le Beau MM, Diaz MO, Hay N (May 1992). "Expression, regulation, and chromosomal localization of the Max gene". Proc Natl Acad Sci U S A. 89 (7): 3111–5. doi:10.1073/pnas.89.7.3111. PMC 48814. PMID 1557420.
  2. ↑ 2.0 2.1 "Entrez Gene: MAX MYC associated factor X".
  3. ↑ Amati B, Land H (February 1994). "Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death". Curr. Opin. Genet. Dev. 4 (1): 102–8. doi:10.1016/0959-437X(94)90098-1. PMID 8193530.
  4. ↑ 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. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  5. ↑ 5.0 5.1 McMahon SB, Wood MA, Cole MD (January 2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc". Mol. Cell. Biol. 20 (2): 556–62. doi:10.1128/MCB.20.2.556-562.2000. PMC 85131. PMID 10611234.
  6. ↑ 6.0 6.1 McMahon SB, Van Buskirk HA, Dugan KA, Copeland TD, Cole MD (August 1998). "The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins". Cell. 94 (3): 363–74. doi:10.1016/S0092-8674(00)81479-8. PMID 9708738.
  7. ↑ Cheng SW, Davies KP, Yung E, Beltran RJ, Yu J, Kalpana GV (May 1999). "c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function". Nat. Genet. 22 (1): 102–5. doi:10.1038/8811. PMID 10319872.
  8. ↑ 8.0 8.1 Mac Partlin M, Homer E, Robinson H, McCormick CJ, Crouch DH, Durant ST, Matheson EC, Hall AG, Gillespie DA, Brown R (February 2003). "Interactions of the DNA mismatch repair proteins MLH1 and MSH2 with c-MYC and MAX". Oncogene. 22 (6): 819–25. doi:10.1038/sj.onc.1206252. PMID 12584560.
  9. ↑ 9.0 9.1 9.2 Blackwood EM, Eisenman RN (Mar 1991). "Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc". Science. UNITED STATES. 251 (4998): 1211–7. doi:10.1126/science.2006410. ISSN 0036-8075. PMID 2006410.
  10. ↑ 10.0 10.1 10.2 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". Proc. Natl. Acad. Sci. U.S.A. 99 (22): 14189–94. doi:10.1073/pnas.232310199. PMC 137859. PMID 12391307.
  11. ↑ 11.0 11.1 Billin AN, Eilers AL, Queva C, Ayer DE (December 1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". J. Biol. Chem. 274 (51): 36344–50. doi:10.1074/jbc.274.51.36344. PMID 10593926.
  12. ↑ 12.0 12.1 Gupta K, Anand G, Yin X, Grove L, Prochownik EV (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene. 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
  13. ↑ 13.0 13.1 13.2 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 (May 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. doi:10.1093/emboj/16.10.2892. PMC 1169897. PMID 9184233.
  14. ↑ 14.0 14.1 Nair SK, Burley SK (January 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. doi:10.1016/S0092-8674(02)01284-9. PMID 12553908.
  15. ↑ 15.0 15.1 15.2 15.3 FitzGerald MJ, Arsura M, Bellas RE, Yang W, Wu M, Chin L, Mann KK, DePinho RA, Sonenshein GE (April 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. doi:10.1038/sj.onc.1202611. PMID 10229200.
  16. ↑ Meroni G, Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A (July 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene. 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. PMID 10918583.
  17. ↑ Ayer DE, Kretzner L, Eisenman RN (January 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. 72 (2): 211–22. doi:10.1016/0092-8674(93)90661-9. PMID 8425218.
  18. ↑ 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 (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  19. ↑ Gupta MP, Amin CS, Gupta M, Hay N, Zak R (July 1997). "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". Mol. Cell. Biol. 17 (7): 3924–36. doi:10.1128/mcb.17.7.3924. PMC 232245. PMID 9199327.
  20. ↑ 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 (July 2011). "Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma". Nat. Genet. 43 (7): 663–7. doi:10.1038/ng.861. PMID 21685915.
  21. ↑ 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 (Dec 2013). "MAX inactivation in small-cell lung cancer disrupts the MYC-SWI/SNF programs and is synthetic lethal with BRG1". Cancer Discov. 4: 292–303. doi:10.1158/2159-8290.CD-13-0799. PMID 24362264.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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