| 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
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
| Transcription factors and intracellular receptors |
|---|
| (1) Basic domains |
| (1.1) Basic leucine zipper (bZIP) |
Activating transcription factor (1, 2, 3, 4, 5, 6) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3) • GABPA • MAF (B, F, G, K) • NRL • NRF1 • XBP1 |
| (1.2) Basic helix-loop-helix (bHLH) |
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BMAL (ARNTL, ARNTL2) • CLOCK • HIF (1A, 3A) • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • NEUROD1 • Twist • USF1 |
| (1.3) bHLH-ZIP |
Myc • MITF • SREBP (1, 2) |
| (1.6) Basic helix-span-helix (bHSH) |
AP-2 |
|
|---|
(2) Zinc finger
DNA-binding domains |
| (2.1) Nuclear receptor (Cys4) |
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP) |
| (2.2) Other Cys4 |
GATA (1, 2, 3, 4, 5, 6) |
| (2.3) Cys2His2 |
General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, TFIIH: 1, 2) • GLI-Krüppel family (1, 2, 3, YY1) • KLF (2, 4, 5, 6, 10, 11, 12, 13) • Sp1 • zinc finger (3, 35, 43, 146, 148, 165, 217, 268, 281, 350) • Zbtb7 (7A) • ZBT (16, 17, 33) |
| (2.4) Cys6 |
HIVEP1 |
|
|---|
(3) Helix-turn-helix
domains |
| (3.1) Homeo domain |
ARX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C6, C8, C9, C13, D1, D3, D4, D9, D10, D11, D12, D13) • NANOG • NKX (2-1, 2-5, 3-1) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) |
| (3.2) Paired box |
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9) |
| (3.3) Fork head / winged helix |
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, L2, M1, N3, O3, O4, P1, P2, P3) |
| (3.4) Heat Shock Factors |
HSF1 |
| (3.5) Tryptophan clusters |
ELF (4, 5) • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB |
| (3.6) TEA domain |
transcriptional enhancer factor 1, 2 |
|
|---|
(4) β-Scaffold factors with
minor groove contacts |
| (4.1) Rel homology region |
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (5, C1, C2, C3, C4) |
| (4.2) STAT |
STAT (1, 2, 3, 4, 5, 6) |
| (4.3) p53 |
p53 |
| (4.4) MADS box |
Mef2 (A, B, C, D) • SRF |
| (4.7) High mobility group |
HNF (1A, 1B) • LEF1 • SOX (3, 4, 6, 9, 10, 13, 18) • SRY • SSRP1 |
| (4.10) Cold-shock domain |
CSDA |
| (4.11) Runt |
CBF (RUNX1, RUNX2, RUNX3) |
|
|---|
(0) Other
transcription factors |
| (0.2) HMGI(Y) |
HMGA (1, 2) |
| (0.3) Pocket domain |
Rb • RBL1 • RBL2 |
| (0.6) Miscellaneous |
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • Rho/Sigma • R-SMAD |
|
|---|
|
