MLL

MLL
Histona-lisina N-metiltransferasa HRX
Protein MLL PDB 2j2s.png
Estructura tridimensional de la proteína MLL.
HUGO 7132
Símbolo MLL
Símbolos alt. ALL-1; CXXC7; HRX; HTRX1; MLL/GAS7; MLL1A; TRX1
Datos genéticos
Locus Cr. 11 q23.3
Bases de datos
Entrez 4297
OMIM 159555
PDB 2j2s
RefSeq NP_005924
UniProt Q03164

La histona-lisina N-metiltransferasa HRX (MLL) es una enzima codificada en humanos por el gen MLL.[1]

MLL es una histona metiltransferasa considerada como un regulador global positivo de la transcripción genética. Esta proteína pertenece al grupo de las enzimas modificadoras de histonas y está implicada en el mantenimiento de las modificaciones epigenéticas de la memoria transcripcional y la patogénesis de la leucemia humana.[2]

MLL también podría participar en la regulación negativa de GAD67 en pacientes con esquizofrenia.[3]

Interacciones

La proteína MLL ha demostrado ser capaz de interaccionar con:

Referencias

  1. Ziemin-van der Poel S, McCabe NR, Gill HJ, Espinosa R 3rd, Patel Y, Harden A, Rubinelli P, Smith SD, LeBeau MM, Rowley JD, et al. (Jan 1992). «Identification of a gene, MLL, that spans the breakpoint in 11q23 translocations associated with human leukemias». Proc Natl Acad Sci U S A 88 (23):  pp. 10735–9. PMID 1720549. 
  2. Guenther MG, Jenner RG, Chevalier B, Nakamura T, Croce CM, Canaani E, Young RA (2005). «Global and Hox-specific roles for the MLL1 methyltransferase». Proc. Natl. Acad. Sci. U.S.A. 102 (24):  pp. 8603–8. doi:10.1073/pnas.0503072102. PMID 15941828. 
  3. Huang HS, Matevossian A, Whittle C, Kim SY, Schumacher A, Baker SP, Akbarian S (2007). «Prefrontal dysfunction in schizophrenia involves mixed-lineage leukemia 1-regulated histone methylation at GABAergic gene promoters». J. Neurosci. 27 (42):  pp. 11254–62. doi:10.1523/JNEUROSCI.3272-07.2007. PMID 17942719. 
  4. a b Xia, Zhen-Biao; Anderson Melanie, Diaz Manuel O, Zeleznik-Le Nancy J (Jul. 2003). «MLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding protein». Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (14):  pp. 8342–7. doi:10.1073/pnas.1436338100. ISSN 0027-8424. PMID 12829790. 
  5. Adler, H T; Chinery R, Wu D Y, Kussick S J, Payne J M, Fornace A J, Tkachuk D C (Oct. 1999). «Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins». Mol. Cell. Biol. (UNITED STATES) 19 (10):  pp. 7050–60. ISSN 0270-7306. PMID 10490642. 
  6. a b c d e Yokoyama, Akihiko; Wang Zhong, Wysocka Joanna, Sanyal Mrinmoy, Aufiero Deborah J, Kitabayashi Issay, Herr Winship, Cleary Michael L (Jul. 2004). «Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression». Mol. Cell. Biol. (United States) 24 (13):  pp. 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. ISSN 0270-7306. PMID 15199122. 
  7. Goto, Natalie K; Zor Tsaffrir, Martinez-Yamout Maria, Dyson H Jane, Wright Peter E (Nov. 2002). «Cooperativity in transcription factor binding to the coactivator CREB-binding protein (CBP). The mixed lineage leukemia protein (MLL) activation domain binds to an allosteric site on the KIX domain». J. Biol. Chem. (United States) 277 (45):  pp. 43168–74. doi:10.1074/jbc.M207660200. ISSN 0021-9258. PMID 12205094. 
  8. Ernst, P; Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. 2001). «MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein». Mol. Cell. Biol. (United States) 21 (7):  pp. 2249–58. doi:10.1128/MCB.21.7.2249-2258.2001. ISSN 0270-7306. PMID 11259575. 
  9. Fair, K; Anderson M, Bulanova E, Mi H, Tropschug M, Diaz M O (May. 2001). «Protein interactions of the MLL PHD fingers modulate MLL target gene regulation in human cells». Mol. Cell. Biol. (United States) 21 (10):  pp. 3589–97. doi:10.1128/MCB.21.10.3589-3597.2001. ISSN 0270-7306. PMID 11313484. 

Enlaces externos


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