| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Although MEF 2 RNAs encoding the MEF2A and MEF2D isoforms are ubiquitously expressed , the presence of MEF 2 proteins in non muscle cell types has been controversial . ^^^ The data show that non muscle MEF 2 complexes contain MEF2A , and that another MEF 2 protein , probably MEF2D , is also present . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Although two of the MADS / MEF2 domain sequences were identical to those of human MEF2A and MEF2D , another domain sequence was similar but not identical to that of human MEF2B . ^^^ While the transcription of MEF2A and MEF2D was up regulated during differentiation of P 19 cells , the MEF2B homologue was abundantly transcribed in undifferentiated P 19 , F 9 and ES cells and down regulated in adult heart , skeletal muscle or brain , suggesting that the murine MEF2B homologue might have a function distinct from other members of the MEF 2 gene family in embryogenesis and development . . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| In normal development , zygotic expression of SL 1 ( MEF2D ) precedes that of SL 2 ( MEF2A ) by several hours , but neither gene is expressed prior to the accumulation of MyoD and Myf 5 transcripts in the somitic mesoderm . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| To begin to assess the roles of the different Mef 2 genes in the control of muscle gene expression in vivo , we analyzed by in situ hybridization the expression patterns of the Mef2a , Mef2c and Mef2d genes during mouse embryogenesis . ^^^ By day 8 . 5 , MEF2A , MEF2C and MEF2D mRNAs are all detected in the myocardium . ^^^ MEF2A and MEF2D are expressed at a lower level than MEF2C in the myotome at day 9 . 5 and are detected in more embryonic tissues than MEF2C . ^^^ The expression of MEF2C in the somites and fetal muscle is distinct from that of MEF2A , MEF2D and the myogenic bHLH regulatory genes , suggesting that it may represent a distinct myogenic cell type . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| On the contrary , we observe that MEF2A , MEF2B , and MEF2D mRNAs are upregulated in the neointima , with the highest levels in the layer of cells nearest to the lumen , whereas MEF2C mRNA levels do not appreciably increase . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| The localization of MEF2A to chromosome 15q26 , MEF2B to 19p12 , MEF2C to 5q14 , and MEF2D to 1q12 q 23 verifies the existence of at least four distinct loci for members of this gene family . . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| By immunofluorescence , we detected abundant nuclear localized MEF2A and MEF2D protein expression in HeLa cells and C2C12 muscle cells . ^^^ Using immuno gel shift analysis and also co immunoprecipitation studies , we show that the predominant MEF 2 DNA binding complex bound to MEF 2 sites from either the muscle creatine kinase or c jun regulatory regions in C2C12 muscle cells is comprised of a MEF2A homodimer , whereas in HeLa cells , it is a MEF2A : MEF2D heterodimer . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| However , MEF2A and MEF2D transcripts have been detected in many adult tissues where they are not translated or the corresponding proteins are rapidly degraded . ^^^ In the present study we have performed in situ immunohistochemistry of whole mount mouse embryos at different stages of development using polyclonal antibodies specific for the MEF2A , MEF2C and MEF2D isoforms . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| In the developing postnatal cerebellum , RNA blot analysis revealed that MEF2A and MEF2D RNA levels increase after birth . ^^^ |
|
| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| We also demonstrate that the protein complex obtained from smooth muscle nuclear extract reacts with MEF2B specific antibody , but not with antibodies specific to MEF2A , MEF2C , or MEF2D , suggesting that only MEF2B protein binds to the A / T rich element . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| In addition , MyoD induced several muscle specific alternative splicings , including structural protein pre mRNAs such as beta tropomyosin and neural cell adhesion molecule and transcriptional protein pre mRNAs such as MEF2A and MEF2D . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| A mutation that blocks this binding markedly reduces gene activation in vivo and in vitro , and overexpression of MEF2A , MEF2C , and MEF2D in noncardiac cells transactivates the cardiac troponin 1 promoter . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Immunoblot analyses of cell lines and primary thymic and splenic lymphocytes show that MEF2C and MEF2D proteins are expressed in B cells and that MEF2D is expressed in T cells ; however , MEF2A protein is not detected in lymphocytes . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| We found that MEF2A , but not MEF2B or MEF2D , is a substrate for p 38 . ^^^ Phosphorylation of MEF2A in a MEF2A MEF2D heterodimer enhances MEF 2 dependent gene expression . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Four family members are known in mammals , referred to as MEF2A , MEF2B , MEF2C , and MEF2D . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Expression of all four MEF 2 transcripts ( MEF2A , MEF2B , MEF2C , and MEF2D ) were detected in all developmental stage of the human heart , while Mef2b transcripts were down regulated in mouse heart development . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Here , we demonstrate that Ca ( 2+ ) activation of MEF 2 response elements in T lymphocytes is mediated in synergy by two Ca ( 2+ ) / calmodulin dependent enzymes , the phosphatase calcineurin , and the kinase type IV / Gr ( CaMKIV / Gr ) , which promote transcription by the MEF 2 family members MEF2A and MEF2D . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| We examined the expression of MEF 2 family members , namely , MEF2A , B , C , and D , in the differentiation of HL 60 promyeloid cells and observed the remarkable increase in the expressions of MEF2A and MEF2D proteins during the differentiation process into monocytes . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Both heart and skeletal muscle were found to express the MEF2A , MEF2C , and MEF2D isoforms but not MEF2B . ^^^ Co immunoprecipitation with isoform specific antibodies revealed that , in the basal state , essentially all of the MEF2A protein was presented as a MEF2A MEF2D heterodimer without any detectable MEF2A MEF2A homodimers or MEF2A MEF2C and MEF2C MEF2D heterodimers . ^^^ Furthermore , immunodepletion of the MEF2A MEF2D complex from control extracts abolished binding to the MEF 2 element . ^^^ These data strongly suggest that the MEF2A MEF2D heterodimer is selectively decreased in insulin deficient diabetes and is responsible for hormonally regulated expression of the GLUT 4 gene . . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Here , we demonstrate that , in addition to MEF2C , BMK 1 phosphorylates and activates MEF2A and MEF2D but not MEF2B . ^^^ The sites phosphorylated by activated BMK 1 were mapped to Ser 355 , Thr 312 , and Thr 319 of MEF2A and Ser 179 of MEF2D both in vitro and in vivo . ^^^ Site directed mutagenesis reveals that the phosphorylation of these sites in MEF2A and MEF2D are necessary for the induction of MEF2A and 2D transactivating activity by either BMK 1 or by epidermal growth factor . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| These adaptations occurred despite the fact that CnA * muscles displayed threefold higher calcineurin activity and enhanced dephosphorylation of the calcineurin targets NFATc 1 , MEF2A , and MEF2D . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| The MEF2A and MEF2D isoforms are differentially regulated in muscle and adipose tissue during states of insulin deficiency . ^^^ Previously we have demonstrated that striated muscle GLUT 4 gene expression decreased following streptozotocin induced diabetes due to a loss of MEF2A transcription factor expression without any significant effect on the MEF2D isoform ( Mora , S . and J . ^^^ In contrast to both cardiac and skeletal muscle , adipose tissue displays a selective decrease in MEF2D expression in diabetes without any significant alteration in MEF2A protein content . ^^^ Furthermore , in vivo overexpression of MEF2A selectively in adipose tissue did not affect GLUT 4 or MEF2D expression and was not sufficient to prevent GLUT 4 down regulation that occurred in insulin deficient states . . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Endogenous MEF2A and MEF2D , but not MEF2B or MEF2C , were phosphorylated with the induction of apoptosis . ^^^ The increased phosphorylation of MEF2A and MEF2D was followed by decreased DNA binding , reduced transcriptional activity , and caspase dependent cleavage to fragments containing N terminal DNA binding domains and C terminal transactivation domains . ^^^ Expression of the highly homologous N terminus of MEF2A ( 1 131 amino acids ) antagonized the transcriptional activity and prosurvival effects of a constitutively active mutant of MEF2D ( MEF2D VP 16 ) . ^^^ We conclude that MEF2A and MEF2D are prosurvival factors with high transcriptional activity in postmitotic cerebellar granule neurons . ^^^ When these neurons are induced to undergo apoptosis by lowering extracellular potassium , MEF2A and MEF2D are phosphorylated , followed by decreased DNA binding and cleavage by a caspase sensitive pathway to N terminal fragments lacking the transactivation domains . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| We show that dephosphorylation of NFATc 1 , MEF2A , and MEF2D transcription factors by calcineurin in all muscle types is dependent on nerve activity and positively correlated with muscle usage under normal weightbearing conditions . ^^^ We also establish that muscle activity must be sustained above native levels for calcineurin dependent dephosphorylation of MEF2A and MEF2D to be transduced into an increase in MEF 2 transcriptional function , suggesting that calcineurin cooperates with other activity linked events to signal via these proteins . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| The caffeine induced increases in GLUT 4 and MEF2A and MEF2D were partially blocked by dantrolene , an inhibitor of sarcoplasmic reticulum Ca ( 2+ ) release , and completely blocked by KN 93 , an inhibitor of Ca ( 2+ ) calmodulin dependent protein kinase ( CAMK ) . ^^^ Caffeine also induced increases in MEF2A , MEF2D , and GLUT 4 in rat epitrochlearis muscles incubated with caffeine in culture medium . 5 Aminoimidazole 4 carboxamide ribonucleoside ( AICAR ) , which activates AMP activated protein kinase ( AMPK ) , also induced approximately twofold increases in GLUT 4 , MEF2A , and MEF2D in L 6 myocytes . ^^^ The data suggest that this effect of Ca ( 2+ ) is mediated by activation of CAMK and indicate that MEF2A and MEF2D are involved in this adaptive response . . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| It was earlier found that p 38 mitogen activated protein ( MAP ) kinase upregulates c jun gene transcription through phosphorylation of two myocyte enhancer factor 2 ( MEF 2 ) family transcription factors , MEF2A and MEF2C , while big MAP kinase 1 ( BMK 1 ) may upregulate c jun gene transcription through MEF2A , MEF2C , and also MEF2D . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Paradoxically , MEF 2 transcriptional activity , revealed by the expression of a MEF 2 dependent transgene , was enhanced in the hearts of Mef2a mutant mice , reflecting the transcriptional activation of residual MEF2D . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Different MEF 2 isoforms expressed in skeletal muscle ( MEF2A , MEF2C , and MEF2D ) and all members of the MyoD family had the capacity to participate in the activity of the GLUT 4 enhancer as assessed by transient transfection in cultured cells . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| The MEF 2 domain binds transcription factors MEF2A and MEF2D in vivo . ^^^ |
|
| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| This site binds myocyte enhancer factor ( MEF ) 2 factors , principally MEF2D and MEF2A in cardiocyte nuclear extracts . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Creatine feeding increased protein levels of myocyte enhancer factor 2 ( MEF 2 ) isoforms MEF2A ( approximately 70 % , P < 0 . 05 ) , MEF2C ( approximately 60 % , P < 0 . 05 ) , and MEF2D ( approximately 90 % , P < 0 . 05 ) , which are transcription factors that regulate GLUT 4 expression , in creatine fed rat EDL muscle nuclear extracts . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| After this , insulin stimulated glycogen synthesis was determined . mRNA levels of the glucose transporters GLUT 1 and GLUT 4 , the peroxisomal proliferator activator receptor gamma ( PPAR gamma ) co activator 1 ( PGC 1 ) and the myocyte specific enhancer factors ( MEF 2 ) , MEF2A , MEF2C and MEF2D were determined using real time PCR analysis after 8 days exposure to the various antidiabetic agents . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation by Cdk 5 alone is sufficient to promote degradation of MEF2A and MEF2D by caspase 3 . ^^^ In contrast to MEF2A and MEF2D , MEF2C is not phosphorylated by Cdk 5 after glutamate exposure and , therefore , resistant to neurotoxin induced caspase dependent degradation . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| NF kappaB , MEF2A , MEF2D and HIF 1 a involvement on insulin and contraction induced regulation of GLUT 4 gene expression in soleus muscle . ^^^ Differently , in vitro , muscle contraction led to a rapid increase ( 35 80 % ) in GLUT 4 , MEF2A , MEF2D and HIF 1 a mRNAs . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| There was no change in nuclear MEF2D or GEF abundance after exercise , but nuclear MEF2A abundance was increased ( P < 0 . 05 ) . ^^^ |
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| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14814 and Q02078 |
Pubmed |
SVM Score :0.0 |
| NA |
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