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Type: Artigo de periódico
Title: Mef2c Dna-binding Activity Is Inhibited Through Its Interaction With The Regulatory Protein Ki-1/57.
Author: Kobarg, Claudia Bandeira
Kobarg, Jörg
Crosara-Alberto, Daniella P
Theizen, Thaís Holtz
Franchini, Kleber Gomes
Abstract: Myocyte 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.
Subject: 14-3-3 Proteins
Amino Acid Sequence
Blotting, Western
Dna-binding Proteins
Electrophoretic Mobility Shift Assay
Escherichia Coli
Fluorescent Antibody Technique
Fluorescent Dyes
Gene Library
Glutathione Transferase
Heart Ventricles
Mads Domain Proteins
Mef2 Transcription Factors
Microscopy, Confocal
Molecular Sequence Data
Myocytes, Cardiac
Myogenic Regulatory Factors
Precipitin Tests
Rats, Wistar
Recombinant Fusion Proteins
Sequence Deletion
Sequence Homology, Amino Acid
Subcellular Fractions
Transcription Factors
Two-hybrid System Techniques
Citation: Febs Letters. v. 579, n. 12, p. 2615-22, 2005-May.
Rights: fechado
Identifier DOI: 10.1016/j.febslet.2005.03.078
Date Issue: 2005
Appears in Collections:Unicamp - Artigos e Outros Documentos

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