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http://dx.doi.org/10.14348/molcells.2017.0116

HDAC11 Inhibits Myoblast Differentiation through Repression of MyoD-Dependent Transcription  

Byun, Sang Kyung (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
An, Tae Hyeon (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Son, Min Jeong (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Lee, Da Som (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Kang, Hyun Sup (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Lee, Eun-Woo (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Han, Baek Soo (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Kim, Won Kon (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Bae, Kwang-Hee (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Oh, Kyoung-Jin (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Lee, Sang Chul (Metabolic Regulation Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Publication Information
Molecules and Cells / v.40, no.9, 2017 , pp. 667-676 More about this Journal
Abstract
Abnormal differentiation of muscle is closely associated with aging (sarcopenia) and diseases such as cancer and type II diabetes. Thus, understanding the mechanisms that regulate muscle differentiation will be useful in the treatment and prevention of these conditions. Protein lysine acetylation and methylation are major post-translational modification mechanisms that regulate key cellular processes. In this study, to elucidate the relationship between myogenic differentiation and protein lysine acetylation/methylation, we performed a PCR array of enzymes related to protein lysine acetylation/methylation during C2C12 myoblast differentiation. Our results indicated that the expression pattern of HDAC11 was substantially increased during myoblast differentiation. Furthermore, ectopic expression of HDAC11 completely inhibited myoblast differentiation, concomitant with reduced expression of key myogenic transcription factors. However, the catalytically inactive mutant of HDAC11 (H142/143A) did not impede myoblast differentiation. In addition, wild-type HDAC11, but not the inactive HDAC11 mutant, suppressed MyoD-induced promoter activities of MEF2C and MYOG (Myogenin), and reduced histone acetylation near the E-boxes, the MyoD binding site, of the MEF2C and MYOG promoters. Collectively, our results indicate that HDAC11 would suppress myoblast differentiation via regulation of MyoD-dependent transcription. These findings suggest that HDAC11 is a novel critical target for controlling myoblast differentiation.
Keywords
HDAC11; lysine acetylation; myoblast differentiation; MyoD-dependent transcription;
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