MEF2C

MEF2C
Identifiers
Aliases	MEF2C, C5DELq14.3, DEL5q14.3, myocyte enhancer factor 2C
External IDs	MGI: 99458 HomoloGene: 31087 GeneCards: MEF2C
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	88,904,257 bp[1]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• protein dimerization activity; • transcription factor activity, sequence-specific DNA binding; • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; • histone deacetylase binding; • transcription factor activity, RNA polymerase II core promoter sequence-specific; • core promoter sequence-specific DNA binding; • transcription regulatory region DNA binding; • RNA polymerase II regulatory region sequence-specific DNA binding; • HMG box domain binding; • activating transcription factor binding; • RNA polymerase II core promoter proximal region sequence-specific DNA binding; • transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; • RNA polymerase II distal enhancer sequence-specific DNA binding; • AT DNA binding; • chromatin binding; • core promoter proximal region sequence-specific DNA binding; • protein binding; • DNA binding; • sequence-specific DNA binding; • protein heterodimerization activity; • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; • RNA polymerase II transcription factor activity, sequence-specific DNA binding;
Cellular component	• cell nucleus; • nuclear speck; • intracellular membrane-bounded organelle; • nucleoplasm; • cytoplasm; • postsynapse; • sarcoplasm; • macromolecular complex; • nuclear chromatin;
Biological process	• negative regulation of neuron apoptotic process; • embryonic skeletal system morphogenesis; • myotube differentiation; • positive regulation of skeletal muscle tissue development; • cell morphogenesis involved in neuron differentiation; • positive regulation of muscle cell differentiation; • regulation of synapse assembly; • muscle organ development; • outflow tract morphogenesis; • monocyte differentiation; • sinoatrial valve morphogenesis; • negative regulation of ossification; • heart looping; • positive regulation of skeletal muscle cell differentiation; • blood vessel remodeling; • cellular response to drug; • blood vessel development; • positive regulation of cardiac muscle cell proliferation; • humoral immune response; • positive regulation of alkaline phosphatase activity; • negative regulation of epithelial cell proliferation; • regulation of synaptic transmission, glutamatergic; • melanocyte differentiation; • apoptotic process; • B cell receptor signaling pathway; • cellular response to calcium ion; • cellular response to transforming growth factor beta stimulus; • renal tubule morphogenesis; • nephron tubule epithelial cell differentiation; • cell fate commitment; • cardiac ventricle formation; • regulation of transcription, DNA-templated; • cardiac muscle cell differentiation; • regulation of neuron apoptotic process; • platelet formation; • neuron development; • smooth muscle cell differentiation; • positive regulation of protein homodimerization activity; • negative regulation of gene expression; • transcription, DNA-templated; • cellular response to trichostatin A; • positive regulation of transcription, DNA-templated; • heart development; • epithelial cell proliferation involved in renal tubule morphogenesis; • cardiac muscle hypertrophy in response to stress; • positive regulation of B cell proliferation; • positive regulation of neuron differentiation; • excitatory postsynaptic potential; • learning or memory; • positive regulation of macrophage apoptotic process; • positive regulation of cardiac muscle cell differentiation; • cellular response to parathyroid hormone stimulus; • primary heart field specification; • secondary heart field specification; • regulation of dendritic spine development; • regulation of germinal center formation; • palate development; • cell differentiation; • chondrocyte differentiation; • positive regulation of bone mineralization; • neural crest cell differentiation; • neuron migration; • B cell homeostasis; • negative regulation of transcription from RNA polymerase II promoter; • endochondral ossification; • regulation of neurotransmitter secretion; • cellular response to fluid shear stress; • nervous system development; • regulation of synaptic plasticity; • regulation of NMDA receptor activity; • muscle cell fate determination; • positive regulation of osteoblast differentiation; • regulation of synaptic activity; • osteoblast differentiation; • neuron differentiation; • regulation of sarcomere organization; • skeletal muscle cell differentiation; • positive regulation of behavioral fear response; • glomerulus morphogenesis; • germinal center formation; • positive regulation of cell proliferation in bone marrow; • MAPK cascade; • regulation of AMPA receptor activity; • multicellular organism development; • B cell proliferation; • positive regulation of gene expression; • positive regulation of myoblast differentiation; • cartilage morphogenesis; • embryonic viscerocranium morphogenesis; • ventricular cardiac muscle cell differentiation; • cellular response to lipopolysaccharide; • skeletal muscle tissue development; • regulation of megakaryocyte differentiation; • positive regulation of transcription from RNA polymerase II promoter; • transcription from RNA polymerase II promoter; • negative regulation of blood vessel endothelial cell migration; • negative regulation of vascular smooth muscle cell proliferation; • negative regulation of vascular associated smooth muscle cell migration; • negative regulation of vascular endothelial cell proliferation;
	Sources:Amigo / QuickGO
Orthologs
	4208
	17260
	ENSG00000081189
	ENSMUSG00000005583
	Q06413
	Q8CFN5
NM_001131005; NM_001193347; NM_001193348; NM_001193349; NM_001193350;
	NM_001308002; NM_002397; NM_001363581
	NM_001170537; NM_025282
NP_001124477; NP_001180276; NP_001180277; NP_001180278; NP_001180279;
	NP_001294931; NP_002388; NP_001350510; NP_001294931.1
NP_001164008; NP_001334493; NP_001334495; NP_001334496; NP_001334497;
	NP_001334498; NP_001334500; NP_001334501; NP_001334502; NP_001334503; NP_001334504; NP_001334505; NP_001334506; NP_001334507; NP_001334508; NP_001334509; NP_001334510; NP_079558
	Wikidata
View/Edit Human	View/Edit Mouse

Myocyte-specific enhancer factor 2C also known as MADS box transcription enhancer factor 2, polypeptide C is a protein that in humans is encoded by the MEF2C gene.^[4]^[5] MEF2C is a transcription factor in the Mef2 family.^[6]^[7]

Genomics

The gene is located at 5q14.3 on the minus (Crick) strand and is 200,723 bases in length. The encoded protein has 473 amino acids with a predicted molecular weight of 51.221 kiloDaltons. Three isoforms have been identified. Several post translational modifications have been identified including phosphorylation on serine-59 and serine-396, sumoylation on lysine-391, acetylation on lysine-4 and proteolytic cleavage.

Interactions

MEF2C has been shown to interact with:

Biological significance

This gene is involved in cardiac morphogenesis and myogenesis and vascular development. It may also be involved in neurogenesis and in the development of cortical architecture. Mice without a functional copy of the Mef2c gene die before birth and have abnormalities in the heart and vascular system.^[15] It is one of the targets of an oncomiR, MIRN21.

In humans mutations of this gene result in autosomal dominant mental retardation 20 (MRD20),^[16] characterised by severe psychomotor impairment, periodic tremor and an abnormal motor pattern with mirror movement of the upper limbs observed during infancy, hypotonia, abnormal EEG, epilepsy, absence of speech, autistic behavior, bruxism, and mild dysmorphic features, mild thinning of the corpus callosum and delay of white matter myelination in the occipital lobes^[17]

MEF2C-binding site is associated with minor allele of SNP rs630923, associated with the risk of multiple sclerosis, and responsible for reduced CXCR5 gene promoter activity in B-cells during activation, that could lead to decreased autoimmune response ^[18]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000081189 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Leifer D, Krainc D, Yu YT, McDermott J, Breitbart RE, Heng J, Neve RL, Kosofsky B, Nadal-Ginard B, Lipton SA (Feb 1993). "MEF2C, a MADS/MEF2-family transcription factor expressed in a laminar distribution in cerebral cortex". Proceedings of the National Academy of Sciences of the United States of America. 90 (4): 1546–50. doi:10.1073/pnas.90.4.1546. PMC 45911. PMID 7679508.
↑ McDermott JC, Cardoso MC, Yu YT, Andres V, Leifer D, Krainc D, Lipton SA, Nadal-Ginard B (Apr 1993). "hMEF2C gene encodes skeletal muscle- and brain-specific transcription factors". Molecular and Cellular Biology. 13 (4): 2564–77. doi:10.1128/mcb.13.4.2564. PMC 359588. PMID 8455629.
↑ Molkentin JD, Black BL, Martin JF, Olson EN (Jun 1996). "Mutational analysis of the DNA binding, dimerization, and transcriptional activation domains of MEF2C". Molecular and Cellular Biology. 16 (6): 2627–36. doi:10.1128/mcb.16.6.2627. PMC 231253. PMID 8649370.
↑ "Entrez Gene: MEF2C myocyte enhancer factor 2C".
↑ Sartorelli V, Huang J, Hamamori Y, Kedes L (Feb 1997). "Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C". Molecular and Cellular Biology. 17 (2): 1010–26. doi:10.1128/mcb.17.2.1010. PMC 231826. PMID 9001254.
↑ Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (Nov 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Molecular and Cellular Biology. 19 (11): 7816–27. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.
↑ Wang AH, Yang XJ (Sep 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Molecular and Cellular Biology. 21 (17): 5992–6005. doi:10.1128/MCB.21.17.5992-6005.2001. PMC 87317. PMID 11486037.
↑ Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Research. 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.
↑ Hosking BM, Wang SC, Chen SL, Penning S, Koopman P, Muscat GE (Sep 2001). "SOX18 directly interacts with MEF2C in endothelial cells". Biochemical and Biophysical Research Communications. 287 (2): 493–500. doi:10.1006/bbrc.2001.5589. PMID 11554755.
↑ Krainc D, Bai G, Okamoto S, Carles M, Kusiak JW, Brent RN, Lipton SA (Oct 1998). "Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1". The Journal of Biological Chemistry. 273 (40): 26218–24. doi:10.1074/jbc.273.40.26218. PMID 9748305.
↑ Maeda T, Gupta MP, Stewart AF (Jun 2002). "TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters". Biochemical and Biophysical Research Communications. 294 (4): 791–7. doi:10.1016/S0006-291X(02)00556-9. PMID 12061776.
↑ Bi W, Drake CJ, Schwarz JJ (Jul 1999). "The transcription factor MEF2C-null mouse exhibits complex vascular malformations and reduced cardiac expression of angiopoietin 1 and VEGF". Developmental Biology. 211 (2): 255–67. doi:10.1006/dbio.1999.9307. PMID 10395786.
↑ Online Mendelian Inheritance in Man (OMIM) 613443
↑ Nowakowska BA, Obersztyn E, Szymańska K, Bekiesińska-Figatowska M, Xia Z, Ricks CB, Bocian E, Stockton DW, Szczałuba K, Nawara M, Patel A, Scott DA, Cheung SW, Bohan TP, Stankiewicz P (Jul 2010). "Severe mental retardation, seizures, and hypotonia due to deletions of MEF2C". American Journal of Medical Genetics Part B. 153B (5): 1042–51. doi:10.1002/ajmg.b.31071. PMID 20333642.
↑ Mitkin NA, Muratova AM, Schwartz AM, Kuprash DV (Nov 2016). "The A Allele of the Single-Nucleotide Polymorphism rs630923 Creates a Binding Site for MEF2C Resulting in Reduced CXCR5 Promoter Activity in B-Cell Lymphoblastic Cell Lines". Front. Immunol. 7 (515). doi:10.3389/fimmu.2016.00515. PMC 5112242. PMID 27909439.

External links

MEF2C+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
FactorBook MEF2C

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000081189 - Ensembl, May 2017

[2] "Human PubMed Reference:".

[3] "Mouse PubMed Reference:".

[pmid7679508-4] Leifer D, Krainc D, Yu YT, McDermott J, Breitbart RE, Heng J, Neve RL, Kosofsky B, Nadal-Ginard B, Lipton SA (Feb 1993). "MEF2C, a MADS/MEF2-family transcription factor expressed in a laminar distribution in cerebral cortex". Proceedings of the National Academy of Sciences of the United States of America. 90 (4): 1546–50. doi:10.1073/pnas.90.4.1546. PMC 45911. PMID 7679508.

[pmid8455629-5] McDermott JC, Cardoso MC, Yu YT, Andres V, Leifer D, Krainc D, Lipton SA, Nadal-Ginard B (Apr 1993). "hMEF2C gene encodes skeletal muscle- and brain-specific transcription factors". Molecular and Cellular Biology. 13 (4): 2564–77. doi:10.1128/mcb.13.4.2564. PMC 359588. PMID 8455629.

[6] Molkentin JD, Black BL, Martin JF, Olson EN (Jun 1996). "Mutational analysis of the DNA binding, dimerization, and transcriptional activation domains of MEF2C". Molecular and Cellular Biology. 16 (6): 2627–36. doi:10.1128/mcb.16.6.2627. PMC 231253. PMID 8649370.

[7] "Entrez Gene: MEF2C myocyte enhancer factor 2C".

[pmid9001254-8] Sartorelli V, Huang J, Hamamori Y, Kedes L (Feb 1997). "Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C". Molecular and Cellular Biology. 17 (2): 1010–26. doi:10.1128/mcb.17.2.1010. PMC 231826. PMID 9001254.

[pmid10523670-9] Wang AH, Bertos NR, Vezmar M, Pelletier N, Crosato M, Heng HH, Th'ng J, Han J, Yang XJ (Nov 1999). "HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor". Molecular and Cellular Biology. 19 (11): 7816–27. doi:10.1128/mcb.19.11.7816. PMC 84849. PMID 10523670.

[pmid11486037-10] Wang AH, Yang XJ (Sep 2001). "Histone deacetylase 4 possesses intrinsic nuclear import and export signals". Molecular and Cellular Biology. 21 (17): 5992–6005. doi:10.1128/MCB.21.17.5992-6005.2001. PMC 87317. PMID 11486037.

[pmid9753748-11] Yang CC, Ornatsky OI, McDermott JC, Cruz TF, Prody CA (Oct 1998). "Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1". Nucleic Acids Research. 26 (20): 4771–7. doi:10.1093/nar/26.20.4771. PMC 147902. PMID 9753748.

[pmid11554755-12] Hosking BM, Wang SC, Chen SL, Penning S, Koopman P, Muscat GE (Sep 2001). "SOX18 directly interacts with MEF2C in endothelial cells". Biochemical and Biophysical Research Communications. 287 (2): 493–500. doi:10.1006/bbrc.2001.5589. PMID 11554755.

[pmid9748305-13] Krainc D, Bai G, Okamoto S, Carles M, Kusiak JW, Brent RN, Lipton SA (Oct 1998). "Synergistic activation of the N-methyl-D-aspartate receptor subunit 1 promoter by myocyte enhancer factor 2C and Sp1". The Journal of Biological Chemistry. 273 (40): 26218–24. doi:10.1074/jbc.273.40.26218. PMID 9748305.

[pmid12061776-14] Maeda T, Gupta MP, Stewart AF (Jun 2002). "TEF-1 and MEF2 transcription factors interact to regulate muscle-specific promoters". Biochemical and Biophysical Research Communications. 294 (4): 791–7. doi:10.1016/S0006-291X(02)00556-9. PMID 12061776.

[15] Bi W, Drake CJ, Schwarz JJ (Jul 1999). "The transcription factor MEF2C-null mouse exhibits complex vascular malformations and reduced cardiac expression of angiopoietin 1 and VEGF". Developmental Biology. 211 (2): 255–67. doi:10.1006/dbio.1999.9307. PMID 10395786.

[16] Online Mendelian Inheritance in Man (OMIM) 613443

[pmid20333642-17] Nowakowska BA, Obersztyn E, Szymańska K, Bekiesińska-Figatowska M, Xia Z, Ricks CB, Bocian E, Stockton DW, Szczałuba K, Nawara M, Patel A, Scott DA, Cheung SW, Bohan TP, Stankiewicz P (Jul 2010). "Severe mental retardation, seizures, and hypotonia due to deletions of MEF2C". American Journal of Medical Genetics Part B. 153B (5): 1042–51. doi:10.1002/ajmg.b.31071. PMID 20333642.

[pmid27909439-18] Mitkin NA, Muratova AM, Schwartz AM, Kuprash DV (Nov 2016). "The A Allele of the Single-Nucleotide Polymorphism rs630923 Creates a Binding Site for MEF2C Resulting in Reduced CXCR5 Promoter Activity in B-Cell Lymphoblastic Cell Lines". Front. Immunol. 7 (515). doi:10.3389/fimmu.2016.00515. PMC 5112242. PMID 27909439.