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30 results on '"Matsuyama, Reiko"'

22. Double PHD Fingers Protein DPF2 Recognizes Acetylated Histones and Suppresses the Function of Estrogen-related Receptor α through Histone Deacetylase 1

Author

Matsuyama, Reiko, primary, Takada, Ichiro, additional, Yokoyama, Atsushi, additional, Fujiyma-Nakamura, Sally, additional, Tsuji, Naoya, additional, Kitagawa, Hirochika, additional, Fujiki, Ryoji, additional, Kim, Misun, additional, Kouzu-Fujita, Madoka, additional, Yano, Tetsu, additional, and Kato, Shigeaki, additional

Published
2010
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23. Retracted: Repressive domain of unliganded human estrogen receptor α associates with Hsc70

Author

Ogawa, Satoko, primary, Oishi, Hajime, additional, Mezaki, Yoshihiro, additional, Kouzu‐Fujita, Madoka, additional, Matsuyama, Reiko, additional, Nakagomi, Madoka, additional, Mori, Eri, additional, Murayama, Emi, additional, Nagasawa, Hiromichi, additional, Kitagawa, Hirochika, additional, Yanagisawa, Junn, additional, Yano, Tetsu, additional, and Kato, Shigeaki, additional

Published
2005
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29. Double PHD fingers protein DPF2 recognizes acetylated histones and suppresses the function of estrogen-related receptor alpha through histone deacetylase 1.

Author

Matsuyama R, Takada I, Yokoyama A, Fujiyma-Nakamura S, Tsuji N, Kitagawa H, Fujiki R, Kim M, Kouzu-Fujita M, Yano T, and Kato S

Subjects
Acetylation, Animals, Cell Differentiation, Cell Nucleus metabolism, DNA-Binding Proteins genetics, Histone Deacetylase 1 genetics, Histones chemistry, Humans, Mice, Mutation, Protein Structure, Tertiary, RNA, Messenger metabolism, Repressor Proteins genetics, Transcription Factors, Transcription, Genetic, Transcriptional Activation, ERRalpha Estrogen-Related Receptor, DNA-Binding Proteins chemistry, Histone Deacetylase 1 chemistry, Receptors, Estrogen chemistry, Repressor Proteins chemistry
Abstract

Estrogen-related receptor alpha (ERRalpha) is a member of the nuclear receptor superfamily and regulates many physiological functions, including mitochondrial biogenesis and lipid metabolism. ERRalpha enhances the transactivation function without endogenous ligand by associating with coactivators such as peroxisome proliferator-activated receptor gamma coactivator 1 alpha and beta (PGC-1alpha and -beta) and members of the steroid receptor coactivator family. However, the molecular mechanism by which the transactivation function of ERRalpha is converted from a repressive state to an active state is poorly understood. Here we used biochemical purification techniques to identify ERRalpha-associated proteins in HeLa cells stably expressing ERRalpha. Interestingly, we found that double PHD fingers protein DPF2/BAF45d suppressed PGC-1alpha-dependent transactivation of ERRalpha by recognizing acetylated histone H3 and associating with HDAC1. DPF2 directly bound to ERRalpha and suppressed the transactivation function of nuclear receptors such as androgen receptor. DPF2 was recruited to ERR target gene promoters in myoblast cells, and knockdown of DPF2 derepressed the level of mRNA expressed by target genes of ERRalpha. These results show that DPF2 acts as a nuclear receptor-selective co-repressor for ERRalpha by associating with both acetylated histone H3 and HDAC1.

Published
2010
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30. Repressive domain of unliganded human estrogen receptor alpha associates with Hsc70.

Author

Ogawa S, Oishi H, Mezaki Y, Kouzu-Fujita M, Matsuyama R, Nakagomi M, Mori E, Murayama E, Nagasawa H, Kitagawa H, Yanagisawa J, Yano T, and Kato S

Subjects
Cells, Cultured, Estrogen Receptor alpha chemistry, Estrogen Receptor alpha genetics, Fluorescent Antibody Technique, Gene Expression Regulation, HSP70 Heat-Shock Proteins genetics, HeLa Cells, Humans, Molecular Chaperones genetics, Molecular Chaperones metabolism, Nuclear Proteins genetics, Nuclear Proteins metabolism, Protein Binding genetics, Protein Interaction Mapping, Protein Structure, Tertiary genetics, Protein Structure, Tertiary physiology, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Repressor Proteins genetics, Transcription, Genetic, Transcriptional Activation genetics, Transfection, Estrogen Receptor alpha metabolism, HSP70 Heat-Shock Proteins metabolism, Ligands, Repressor Proteins metabolism
Abstract

Estrogen receptor (ER) is a hormone-inducible transcription factor as a member of the nuclear receptor gene superfamily. Unliganded ER is transcriptionally silent and capable of DNA binding; however, it is unable to suppress the basal activity of the target gene promoters, unlike non-steroid hormone receptors that associate with corepressors in the absence of their cognate ligands. To study the molecular basis of how unliganded human ERalpha is maintained silent in gene regulation upon the target gene promoters, we biochemically searched interactants for hERalpha, and identified heat shock protein 70 (Hsc70). Hsc70 appeared to associate with the N-terminal hormone binding E domain, that also turned out a transcriptionally repressive domain. Competitive association of Hsc70 with a best known coactivator p300 was observed. Thus, these findings suggest that Hsc70 associates with unliganded hERalpha, and thereby deters hERalpha from recruiting transcriptional coregulators, presumably as a component of chaperone complexes.

Published
2005
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