Mef2c Dna-binding Activity Is Inhibited Through Its Interaction With The Regulatory Protein Ki-1/57.

dc.creatorKobarg, Claudia Bandeira
dc.creatorKobarg, Jörg
dc.creatorCrosara-Alberto, Daniella P
dc.creatorTheizen, Thaís Holtz
dc.creatorFranchini, Kleber Gomes
dc.date2005-May
dc.date2015-11-27T13:02:03Z
dc.date2015-11-27T13:02:03Z
dc.date.accessioned2018-03-29T01:00:46Z
dc.date.available2018-03-29T01:00:46Z
dc.identifierFebs Letters. v. 579, n. 12, p. 2615-22, 2005-May.
dc.identifier0014-5793
dc.identifier10.1016/j.febslet.2005.03.078
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/15862299
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/196242
dc.identifier15862299
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1296475
dc.descriptionMyocyte enhancer factor (MEF2) are MADS box transcription factors that play important roles in the regulation of myogenesis and morphogenesis of muscle cells. MEF2 proteins are activated by mechanical overload in the heart. In this study, we found the interaction of MEF2C with the regulatory protein Ki-1/57 using yeast two-hybrid system. This interaction was confirmed by GST-pull down assay in vitro and by co-immunoprecipitation in vivo. This interaction is also dependent on pressure overload in the heart. Co-imunoprecipitation assay with anti-MEF2 and anti-Ki-1/57 antibodies demonstrated a basal association between these proteins in the left ventricles of control rats. Pressure overload caused a reduction in this association. Ki-1/57 co-localizes with MEF2 in the nucleus of myocytes of control rats. However, after submitting the animals to pressure overload Ki-1/57 leaves the nucleus thereby decreasing this co-localization. Ki-1/57 also exerts an inhibitory effect upon MEF2C DNA binding activity. These results suggest that Ki-1/57 is a new interacting partner of MEF2 protein and may be involved in the regulation of MEF2 at the onset of hypertrophy.
dc.description579
dc.description2615-22
dc.languageeng
dc.relationFebs Letters
dc.relationFEBS Lett.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subject14-3-3 Proteins
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectBlotting, Western
dc.subjectDna
dc.subjectDna-binding Proteins
dc.subjectElectrophoretic Mobility Shift Assay
dc.subjectEscherichia Coli
dc.subjectFluorescent Antibody Technique
dc.subjectFluorescent Dyes
dc.subjectGene Library
dc.subjectGlutathione Transferase
dc.subjectHeart Ventricles
dc.subjectHumans
dc.subjectHydrazines
dc.subjectImmunohistochemistry
dc.subjectMads Domain Proteins
dc.subjectMef2 Transcription Factors
dc.subjectMale
dc.subjectMicroscopy, Confocal
dc.subjectMolecular Sequence Data
dc.subjectMyocytes, Cardiac
dc.subjectMyogenic Regulatory Factors
dc.subjectPrecipitin Tests
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectRecombinant Fusion Proteins
dc.subjectSequence Deletion
dc.subjectSequence Homology, Amino Acid
dc.subjectSubcellular Fractions
dc.subjectTranscription Factors
dc.subjectTwo-hybrid System Techniques
dc.titleMef2c Dna-binding Activity Is Inhibited Through Its Interaction With The Regulatory Protein Ki-1/57.
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución