The MEF2B Homolog Differentially Expressed in Mouse Embryonal Carcinoma Cells

Hidaka, Kumi; Morisaki, T.; Byun, Sang-Hyun; Hashido, Kazuo; Toyama, Keiko; Mukai, Tokuo

doi:10.1006/bbrc.1995.2167

Cited by 17 publications

(14 citation statements)

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“…We detected no significant nucleotide sequence homology between mouse and human MEF2 cDNAs in the 5Ј untranslated regions. While this work was in preparation, the sequence of MEF2B was published by another group (14). The open reading frame of their sequence agrees with ours.…”

Section: Mef2b Is the Most Divergent Of The Vertebrate Mef2 Factorssupporting

confidence: 81%

MEF2B Is a Potent Transactivator Expressed in Early Myogenic Lineages

Molkentin

Firulli

Black

et al. 1996

Molecular and Cellular Biology

122

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There are four members of the myocyte enhancer binding factor 2 (MEF2) family of transcription factors, MEF2A, -B, -C, and -D, that have homology within an amino-terminal MADS box and an adjacent MEF2 domain that together mediate dimerization and DNA binding. MEF2A, -C, and -D have previously been shown to bind an A/T-rich DNA sequence in the control regions of numerous muscle-specific genes, whereas MEF2B was reported to be unable to bind this sequence unless the carboxyl terminus was deleted. To further define the functions of MEF2B, we analyzed its DNA binding and transcriptional activities. In contrast to previous studies, our results show that MEF2B binds the same DNA sequence as other members of the MEF2 family and acts as a strong transactivator through that sequence. Transcriptional activation by MEF2B is dependent on the carboxyl terminus, which contains two conserved sequence motifs found in all vertebrate MEF2 factors. During mouse embryogenesis, MEF2B transcripts are expressed in the developing cardiac and skeletal muscle lineages in a temporospatial pattern distinct from but overlapping with those of the other Mef2 genes. The mouse Mef2b gene maps to chromosome 8 and is unlinked to other Mef2 genes; its intron-exon organization is similar to that of the other vertebrate Mef2 genes and the single Drosophila Mef2 gene, consistent with the notion that these different Mef2 genes evolved from a common ancestral gene.The myocyte enhancer binding factor 2 (MEF2) family comprises a group of transcription factors that have homology within a MADS (MCM1-agamous-deficients-serum response factor) box at their amino termini and an adjacent motif known as the MEF2 domain (reviewed in reference 39). There are four Mef2 genes in vertebrates, Mef2a-d, whose products bind as homo-and heterodimers to the A/T-rich DNA sequence CTA(A/T) 4 TAG/A (2, 3, 5, 20, 29-31, 41, 50). MEF2 binding sites were first identified in the control regions of musclespecific genes, where they are required for transcriptional activation (8). More recently, they have also been shown to be important for serum inducibility of the c-jun gene (10, 11). There is a single Mef2 gene, D-mef2, in Drosophila melanogaster, which encodes a protein with the same DNA binding properties as the vertebrate MEF2 factors (21, 37). This gene has been shown to be required for differentiation of skeletal, cardiac, and visceral muscle cells in the Drosophila embryo (1, 22, 42).The MADS and MEF2 domains mediate DNA binding and dimerization of MEF2 monomers (33, 41). MEF2 factors can also interact with heterodimers formed between myogenic basic helix-loop-helix (bHLH) factors, such as MyoD and myogenin, and ubiquitous bHLH proteins (32). Amino acids in the MADS and MEF2 domains appear to be the primary determinants of this type of protein-protein interaction (32). MEF2A, -C, and -D show similar DNA binding and transcriptional activation properties (2, 29-31, 41, 50). In contrast, it has been reported that human MEF2B is unable to bind the MEF2 consensus sequence unles...

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Section: Mef2b Is the Most Divergent Of The Vertebrate Mef2 Factorssupporting

confidence: 81%

MEF2B Is a Potent Transactivator Expressed in Early Myogenic Lineages

Molkentin

Firulli

Black

et al. 1996

Molecular and Cellular Biology

122

View full text Add to dashboard Cite

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“…Haspin has a region homologous to MEF2B at residues 144 -162 (38) and similarly has a basic amino acid region at its N terminus. The mef2B gene encodes a MADS box transcription factor, which regulates the expression of many muscle-specific genes (43).…”

Section: Ectopic Expression Of Haspin Inhibits Proliferation Of Hek-2mentioning

confidence: 99%

Identification and Characterization of a Haploid Germ Cell-specific Nuclear ProteinKinase (Haspin) in Spermatid Nuclei and Its Effects on Somatic Cells

Tanaka¹,

Yoshimura²,

Nozaki³

et al. 1999

Journal of Biological Chemistry

110

111

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We have cloned the entire coding region of a mouse germ cell-specific cDNA encoding a unique protein kinase whose catalytic domain contains only three consensus subdomains (I-III) instead of the normal 12. The protein possesses intrinsic Ser/Thr kinase activity and is exclusively expressed in haploid germ cells, localizing only in their nuclei, and was thus named Haspin (for haploid germ cell-specific nuclear protein kinase). Western blot analysis showed that specific antibodies recognized a protein of M r 83,000 in the testis. Ectopically expressed Haspin was detected exclusively in the nuclei of cultured somatic cells. Even in the absence of kinase activity, however, Haspin caused cell cycle arrest at G 1 , resulting in growth arrest of the transfected somatic cells. In a DNA binding experiment, approximately onehalf of wild-type Haspin was able to bind to a DNAcellulose column, whereas the other half was not. In contrast, all of the deletion mutant Haspin that lacked autophosphorylation bound to the DNA column. Thus, the DNA-binding activity of Haspin may, in some way, be associated with its kinase activity. These observations suggest that Haspin has some critical roles in cell cycle cessation and differentiation of haploid germ cells.

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“…최근에 박 등 . MEF2는 생쥐 배아의 carcinoma P19 세포의 분 화 과정 중에 발현이 증가 11) 되고, 발육중인 근육세포에서도 그 발현이 증가 12) 하기 때문에 근육세포의 증식과 종양의 증 식 조절자로 작용하는 것으로 여겨진다.…”

Section: Rt-pcrunclassified

“…따라서 단백질칩을 이용한 APin의 protein microarray는 APin과 상호작용하는 단백 질들을 분석하는 적절한 방법으로 이용될 수 있다. 본 연구 에서는 protein microarray를 이용하여 APin 단백질과 높 은 친화성을 나타낸 74개의 단백질 중에서 치아 발생이나 석회화 연관되는 전사인자나 분화 유도인자들을 선택하였 다. MADS box transcription enhancer factor 2 (MEF2) 11,12) 와 Aurora kinase A [13][14][15] 는 종양의 생성 (tumorigenesis)과 증식 (tumor proliferation)에 관계가 있는 전사인자이고, bone morphogenetic protein receptor IB (BMPR-IB) 16,17) 는 다양한 기관의 발생과정에 관여 하고, EF-hand calcium binding protein 18,19) 는 다양한 세 포들의 석회화(mineralization) 과정에 연관된 것으로 알 려져 있다.…”

unclassified

A study of APin-protein interactions using protein microarray

Park

Kim

et al. 2007

J Korean Acad Conserv Dent

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Protein microarray or protein chips is potentially powerful tools for analysis of protein-protein interactions. APin cDNA was previously identified and cloned from a rat odontoblast cDNA library. The purpose of this study was to investigate the APin-protein interactions during ameloblast differentiation. Protein microarray was carried with recombinant APin protein and MEF2, Aurora kinase A, BMPR-IB and EFhand calcium binding protein were selected among 74 interacting proteins. Immortalized ameloblast cells (ALCs) were transfected with pCMV-APin construct and U6-APin siRNA construct. After transfection, the expression of the mRNAs for four proteins selected by protein micoarrays were assessed by RT-PCR.The results were as follows: 1. APin expression was increased and decreased markedly after its over-expression and inactivation, respectively. 2. Over-expression of the APin in the ALCs markedly down-regulated the expression of MEF2 and Aurora kinase A, whereas their expression remained unchanged by its inactivation. 3. Expression of BMPR-IB and EF-hand calcium binding protein were markedly increased by the overexpression of the APin in the ALCs, whereas expression of BMPR-IB remained unchanged and expression of EF-hand calcium binding protein was markedly decreased by its inactivation. These results suggest that APin plays an important role in ameloblast differentiation and mineralization by regulating the expression of MEF2, Aurora kinase A, BMPR-IB and EF-hand calcium binding protein.[J Kor Acad Cons Dent 32(5): [459][460][461][462][463][464][465][466][467][468] 2007]

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The MEF2B Homolog Differentially Expressed in Mouse Embryonal Carcinoma Cells

Cited by 17 publications

References 0 publications

MEF2B Is a Potent Transactivator Expressed in Early Myogenic Lineages

MEF2B Is a Potent Transactivator Expressed in Early Myogenic Lineages

Identification and Characterization of a Haploid Germ Cell-specific Nuclear ProteinKinase (Haspin) in Spermatid Nuclei and Its Effects on Somatic Cells

A study of APin-protein interactions using protein microarray

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