MAD protein is a protein that in humans is encoded by the MXD1gene.[1][2]
MAD-MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acts as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor.[2] The MAD-MAX protein dimer may be a reference to the popular cult classic film Mad Max (1979).
↑Shapiro DN, Valentine V, Eagle L, Yin X, Morris SW, Prochownik EV (February 1995). "Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25". Genomics. 23 (1): 282–5. doi:10.1006/geno.1994.1496. PMID7829091.
↑Laherty, C D; Yang W M; Sun J M; Davie J R; Seto E; Eisenman R N (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. UNITED STATES. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. ISSN0092-8674. PMID9150134.
↑Spronk, C A; Tessari M; Kaan A M; Jansen J F; Vermeulen M; Stunnenberg H G; Vuister G W (December 2000). "The Mad1-Sin3B interaction involves a novel helical fold". Nat. Struct. Biol. UNITED STATES. 7 (12): 1100–4. doi:10.1038/81944. ISSN1072-8368. PMID11101889.
↑ 5.05.1Gupta, K; Anand G; Yin X; Grove L; Prochownik E V (March 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. ISSN0950-9232. PMID9528857.
↑Cairo, S; Merla G; Urbinati F; Ballabio A; Reymond A (March 2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Hum. Mol. Genet. England. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. ISSN0964-6906. PMID11230181.
↑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. ENGLAND. 19 (29): 3266–77. doi:10.1038/sj.onc.1203634. ISSN0950-9232. PMID10918583.
↑Swanson, Kurt A; Knoepfler Paul S; Huang Kai; Kang Richard S; Cowley Shaun M; Laherty Carol D; Eisenman Robert N; Radhakrishnan Ishwar (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nat. Struct. Mol. Biol. United States. 11 (8): 738–46. doi:10.1038/nsmb798. ISSN1545-9993. PMID15235594.
↑Brubaker, K; Cowley S M; Huang K; Loo L; Yochum G S; Ayer D E; Eisenman R N; Radhakrishnan I (November 2000). "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex". Cell. UNITED STATES. 103 (4): 655–65. doi:10.1016/S0092-8674(00)00168-9. ISSN0092-8674. PMID11106735.
↑Ayer, D E; Lawrence Q A; Eisenman R N (March 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. UNITED STATES. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. ISSN0092-8674. PMID7889570.
↑Ayer, D E; Kretzner L; Eisenman R N (January 1993). "Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity". Cell. UNITED STATES. 72 (2): 211–22. doi:10.1016/0092-8674(93)90661-9. ISSN0092-8674. PMID8425218.
↑Nair, Satish K; Burley Stephen K (January 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. doi:10.1016/S0092-8674(02)01284-9. ISSN0092-8674. PMID12553908.
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 (1): 653–99. doi:10.1146/annurev.cellbio.16.1.653. PMID11031250.
Ayer DE, Lawrence QA, Eisenman RN (1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. PMID7889570.
Edelhoff S, Ayer DE, Zervos AS, et al. (1994). "Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins: MAD to human chromosome 2 and mouse chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome 19". Oncogene. 9 (2): 665–8. PMID8290278.
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. PMID8425218.
Hassig CA, Fleischer TC, Billin AN, et al. (1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID9150133.
Laherty CD, Yang WM, Sun JM, et al. (1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. PMID9150134.
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. PMID9528857.
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. PMID10229200.
Khan MM, Nomura T, Kim H, et al. (2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Mol. Cell. 7 (6): 1233–43. doi:10.1016/S1097-2765(01)00257-X. PMID11430826.
Nikiforov MA, Popov N, Kotenko I, et al. (2003). "The Mad and Myc basic domains are functionally equivalent". J. Biol. Chem. 278 (13): 11094–9. doi:10.1074/jbc.M212298200. PMID12538578.
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. doi:10.1016/S0092-8674(02)01284-9. PMID12553908.
Siegel PM, Shu W, Massagué J (2003). "Mad upregulation and Id2 repression accompany transforming growth factor (TGF)-beta-mediated epithelial cell growth suppression". J. Biol. Chem. 278 (37): 35444–50. doi:10.1074/jbc.M301413200. PMID12824180.
Zada AA, Pulikkan JA, Bararia D, et al. (2007). "Proteomic discovery of Max as a novel interacting partner of C/EBPalpha: a Myc/Max/Mad link". Leukemia. 20 (12): 2137–46. doi:10.1038/sj.leu.2404438. PMID17082780.