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MYC associated factor X

PDB rendering based on 1an2.
Available structures
1an2, 1hlo, 1nkp, 1nlw, 1r05
Identifiers
Symbols MAX; MGC10775; MGC11225; MGC18164; MGC34679; MGC36767; orf1
External IDs OMIM154950 MGI96921 HomoloGene1786 GeneCards: MAX Gene
RNA expression pattern
PBB GE MAX 214108 at tn.png
PBB GE MAX 208403 x at tn.png
PBB GE MAX 209331 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4149 17187
Ensembl ENSG00000125952 n/a
UniProt P61244 n/a
RefSeq (mRNA) NM_002382 XM_001002021
RefSeq (protein) NP_002373 XP_001002021
Location (UCSC) Chr 14:
64.54 - 64.64 Mb
n/a
PubMed search [1] [2]

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

Contents

Function

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]

Interactions

MAX (gene) has been shown to interact with MSH2,[3] MXD1,[4][5][6][7] MXI1,[8][9][6][10][11] SPAG9,[4] N-Myc,[12][11] MYCL1,[12][11] Myc,[13][14][15][16][3][12][4][9][6][10][7][11][17] Transformation/transcription domain-associated protein,[14][15] MNT[10] and TEAD1.[18]

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. PMID 1557420.  
  2. ^ a b "Entrez Gene: MAX MYC associated factor X". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4149.  
  3. ^ a b Mac Partlin, Mary; Homer Elizabeth, Robinson Helen, McCormick Carol J, Crouch Dorothy H, Durant Stephen T, Matheson Elizabeth C, Hall Andrew G, Gillespie David A F, Brown Robert (Feb. 2003). "Interactions of the DNA mismatch repair proteins MLH1 and MSH2 with c-MYC and MAX". Oncogene (England) 22 (6): 819–25. doi:10.1038/sj.onc.1206252. ISSN 0950-9232. PMID 12584560.  
  4. ^ a b c Lee, Clement M; Onésime Djamila, Reddy C Damodara, Dhanasekaran N, Reddy E Premkumar (Oct. 2002). "JLP: A scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (22): 14189–94. doi:10.1073/pnas.232310199. ISSN 0027-8424. PMID 12391307.  
  5. ^ Ayer, D E; Kretzner L, Eisenman R N (Jan. 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell (UNITED STATES) 72 (2): 211–22. ISSN 0092-8674. PMID 8425218.  
  6. ^ a b c Gupta, K; Anand G, Yin X, Grove L, Prochownik E V (Mar. 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene (ENGLAND) 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. ISSN 0950-9232. PMID 9528857.  
  7. ^ a b Nair, Satish K; Burley Stephen K (Jan. 2003). "X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors". Cell (United States) 112 (2): 193–205. ISSN 0092-8674. PMID 12553908.  
  8. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.  
  9. ^ a b Billin, A N; Eilers A L, Queva C, Ayer D E (Dec. 1999). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". J. Biol. Chem. (UNITED STATES) 274 (51): 36344–50. ISSN 0021-9258. PMID 10593926.  
  10. ^ a b c Meroni, G; Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter D H, 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. (ENGLAND) 16 (10): 2892–906. doi:10.1093/emboj/16.10.2892. ISSN 0261-4189. PMID 9184233.  
  11. ^ a b c d FitzGerald, M J; Arsura M, Bellas R E, Yang W, Wu M, Chin L, Mann K K, DePinho R A, Sonenshein G E (Apr. 1999). "Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc". Oncogene (ENGLAND) 18 (15): 2489–98. doi:10.1038/sj.onc.1202611. ISSN 0950-9232. PMID 10229200.  
  12. ^ a b c Blackwood, E M; Eisenman R N (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. ISSN 0036-8075. PMID 2006410.  
  13. ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3: 89. doi:10.1038/msb4100134. PMID 17353931.  
  14. ^ a b McMahon, S B; Wood M A, Cole M D (Jan. 2000). "The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc". Mol. Cell. Biol. (UNITED STATES) 20 (2): 556–62. ISSN 0270-7306. PMID 10611234.  
  15. ^ a b McMahon, S B; Van Buskirk H A, Dugan K A, Copeland T D, Cole M D (Aug. 1998). "The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins". Cell (UNITED STATES) 94 (3): 363–74. ISSN 0092-8674. PMID 9708738.  
  16. ^ Cheng, S W; Davies K P, Yung E, Beltran R J, Yu J, Kalpana G V (May. 1999). "c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function". Nat. Genet. (UNITED STATES) 22 (1): 102–5. doi:10.1038/8811. ISSN 1061-4036. PMID 10319872.  
  17. ^ Meroni, G; Cairo S, Merla G, Messali S, Brent R, Ballabio A, Reymond A (Jul. 2000). "Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?". Oncogene (ENGLAND) 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. ISSN 0950-9232. PMID 10918583.  
  18. ^ Gupta, M P; Amin C S, Gupta M, Hay N, Zak R (Jul. 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. (UNITED STATES) 17 (7): 3924–36. ISSN 0270-7306. PMID 9199327.  

Further reading

  • Grandori C, Cowley SM, James LP, Eisenman RN (2001). "The Myc/Max/Mad network and the transcriptional control of cell behavior.". Annu. Rev. Cell Dev. Biol. 16: 653–99. doi:10.1146/annurev.cellbio.16.1.653. PMID 11031250.  
  • Lüscher B (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.  
  • Wechsler DS, Dang CV (1992). "Opposite orientations of DNA bending by c-Myc and Max.". Proc. Natl. Acad. Sci. U.S.A. 89 (16): 7635–9. doi:10.1073/pnas.89.16.7635. PMID 1323849.  
  • Mäkelä TP, Koskinen PJ, Västrik I, Alitalo K (1992). "Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation.". Science 256 (5055): 373–7. doi:10.1126/science.256.5055.373. PMID 1566084.  
  • Gilladoga AD, Edelhoff S, Blackwood EM, et al. (1992). "Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in situ hybridization.". Oncogene 7 (6): 1249–51. PMID 1594250.  
  • 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. doi:10.1126/science.2006410. PMID 2006410.  
  • Zervos AS, Faccio L, Gatto JP, et al. (1995). "Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein.". Proc. Natl. Acad. Sci. U.S.A. 92 (23): 10531–4. doi:10.1073/pnas.92.23.10531. PMID 7479834.  
  • Bousset K, Henriksson M, Lüscher-Firzlaff JM, et al. (1993). "Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers.". Oncogene 8 (12): 3211–20. PMID 8247525.  
  • Ayer DE, Kretzner L, Eisenman RN (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.  
  • Västrik I, Koskinen PJ, Alitalo R, Mäkelä TP (1993). "Alternative mRNA forms and open reading frames of the max gene.". Oncogene 8 (2): 503–7. PMID 8426752.  
  • Ferré-D'Amaré AR, Prendergast GC, Ziff EB, Burley SK (1993). "Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.". Nature 363 (6424): 38–45. doi:10.1038/363038a0. PMID 8479534.  
  • Hurlin PJ, Quéva C, Koskinen PJ, et al. (1996). "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation.". Embo J. 14 (22): 5646–59. PMID 8521822.  
  • Grandori C, Mac J, Siëbelt F, et al. (1996). "Myc-Max heterodimers activate a DEAD box gene and interact with multiple E box-related sites in vivo.". Embo J. 15 (16): 4344–57. PMID 8861962.  
  • Brownlie P, Ceska T, Lamers M, et al. (1997). "The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control.". Structure 5 (4): 509–20. doi:10.1016/S0969-2126(97)00207-4. PMID 9115440.  
  • Meroni G, Reymond A, Alcalay M, et al. (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. PMID 9184233.  
  • Gupta MP, Amin CS, Gupta M, et al. (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. PMID 9199327.  
  • Gupta K, Anand G, Yin X, et al. (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.  
  • Lavigne P, Crump MP, Gagné SM, et al. (1998). "Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.". J. Mol. Biol. 281 (1): 165–81. doi:10.1006/jmbi.1998.1914. PMID 9680483.  
  • FitzGerald MJ, Arsura M, Bellas RE, et al. (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.  

External links

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

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