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Mef2



myocyte enhancer factor 2A
Identifiers
Symbol MEF2A
Entrez 4205
HUGO 6993
OMIM 600660
RefSeq NM_005587
UniProt Q02078
Other data
Locus Chr. 15 q26
myocyte enhancer factor 2B
Identifiers
Symbol MEF2B
Entrez 4207
HUGO 6995
OMIM 600661
RefSeq NM_005919
UniProt Q02080
Other data
Locus Chr. 19 p13.11
myocyte enhancer factor 2C
Identifiers
Symbol MEF2C
Entrez 4208
HUGO 6996
OMIM 600662
RefSeq NM_002397
UniProt Q06413
Other data
Locus Chr. 5 q14
myocyte enhancer factor 2D
Identifiers
Symbol MEF2D
Entrez 4209
HUGO 6997
OMIM 600663
RefSeq NM_005920
UniProt Q14814
Other data
Locus Chr. 1 q12-q23

Myocyte Enhancer Factor-2 (MEF2) is a transcription factor or family of transcription factors that contain both the MADS-box and MEF2 DNA-binding domains. Many, if not all, members of the MEF2 family are required for proper development of an embryo.

Additional recommended knowledge


MEF2 was originally identified as a transcription factor in Drosophila (sometimes called D-MEF2) through promoter analysis of the muscle creatine kinase (mck) gene to identify nuclear factors interacting with the mck enhancer region.

While Drosophila has the single MEF2 gene, Vertebrates have four versions of the Mef2 gene (Mef2a, Mef2b, Mef2c, and Mef2d), all expressed in distinct but overlapping patterns during embryogenesis through adulthood.[1] All of the mammalian Mef2 genes share approximately 50% overall amino acid identity and about 95% similarity throughout the highly conserved N-terminal MADS-box and MEF2 domains, however their sequences diverge in their C-terminal transactivation domain.[2] The MADS-box serves as the minimal DNA-binding domain, however an adjacent 29-amino acid extension called the MEF2 domain is required for high affinity DNA-binding and dimerization. Through an interaction with the MADS-box, MEF2 transcription factors have the ability to homo- and heterodimerize,[3] and a classic nuclear localization sequence (NLS) in the C-terminus of MEF2A, -C, and – D ensures nuclear localization of the protein.[4] Interestingly, D-MEF2 and MEF2B lack this conserved NLS but are still found in the nucleus.[5]


References

  1. ^ McKinsey TA, Zhang CL, Olson EN (2002). "MEF2: a calcium-dependent regulator of cell division, differentiation and death". Trends Biochem Sci. 27 (1): 40-7. PMID 11796223.
  2. ^ Black BL, Olson EN (1998). "Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins". Annu Rev Cell Dev Biol 14: 167-96. PMID 9891782.
  3. ^ Molkentin JD, Olson EN (1996). "Combinatorial control of muscle development by basic helix-loop-helix and MADS-box transcription factors". Proc Natl Acad Sci U S A 93 (18): 9366-73. PMID 8790335.
  4. ^ Borghi S, Molinari S, Razzini G, Parise F, Battini R, Ferrari S (2001). "The nuclear localization domain of the MEF2 family of transcription factors shows member-specific features and mediates the nuclear import of histone deacetylase 4". J Cell Sci 114: 4477-83. PMID 11792813.
  5. ^ Yu YT (1996). "Distinct domains of myocyte enhancer binding factor-2A determining nuclear localization and cell type-specific transcriptional activity". J Biol Chem 271 (40): 24675-83. PMID 8798735.


 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Mef2". A list of authors is available in Wikipedia.
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