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Expression data from transgenic mice overexpressing RXR-gamma in the skeletal muscle (RXR-gamma mice)

ABSTRACT: Retinoid X receptor (RXR)-gamma is a nuclear receptor-type transcription factor expressed mostly in the skeletal muscle, and regulated by nutritional conditions. Previously, we established transgenic mice overexpressing RXR-gamma in the skeletal muscle (RXR-gamma mice), which showed lower blood glucose than the control mice. We used microarrays to investigate their glucose metabolism gene expression change. RNA was isolated from the skeletal muscle of sex- and age-matched RXR-gamma mice and non-transgenic control mice (females at 4 months of age, five samples from each group were combined). Each of the combined samples of the two groups was hybridized to the Affymetrix MG430 microarray.

ORGANISM(S): Mus musculus

SUBMITTER: Takako Takai

PROVIDER: E-GEOD-28447 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Expression data from transgenic mice overexpressing RXR-gamma in the skeletal muscle (RXR-gamma mice)

Project description:Retinoid X receptor (RXR)-gamma is a nuclear receptor-type transcription factor expressed mostly in the skeletal muscle, and regulated by nutritional conditions. Previously, we established transgenic mice overexpressing RXR-gamma in the skeletal muscle (RXR-gamma mice), which showed lower blood glucose than the control mice. We used microarrays to investigate their glucose metabolism gene expression change.

2011-04-08 | GSE28447 | GEO

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2008-12-10 | E-GEOD-13511 | biostudies-arrayexpress

Structural basis for DNA recognition and allosteric control of the Retinoic Acid Receptors RAR-RXR

Project description:Retinoic Acid Receptors (RARs) as a functional heterodimer with Retinoid X Receptors (RXRs), bind a diverse series of RA-response elements (RAREs) in regulated genes. Among them, the non-canonical DR0 elements are bound by RXR-RAR with comparable affinities to DR5 elements but DR0 elements do not act transcriptionally as independent RAREs. In this work, we present structural insight for the recognition of DR5 and DR0 elements by RXR-RAR heterodimer using x-ray crystallography, small angle x-ray scattering, and hydrogen/deuterium exchange coupled to mass spectrometry. We solved the crystal structure of RXR-RAR DNA-binding domain in complex with the Rarb2 DR5 and RXR DNA-binding domain in complex with Hoxb13 DR0. While cooperative binding was observed on DR5, on DR0 the two molecules bound non-cooperatively on opposite sides of the DNA. In addition, our data unveil the structural organization and dynamics of the multi-domain RXR-RAR DNA complexes providing evidence for DNA-dependent allosteric communication between domains. Differential binding mode between DR0 and DR5 were observed leading to differences in the conformation and structural dynamics of the multi-domain RXR-RAR DNA complex. These results reveal that the topological organization of the RAR binding element confer regulatory information by modulating the overall topology and structural dynamics of the RXR-RAR heterodimers.

2021-02-10 | PXD018172 | Pride

Mus musculus

Project description:Expression data from transgenic mice overexpressing RXR-gamma in the skeletal muscle (RXR-gamma mice)

| PRJNA139261 | ENA

Genome-wide profiling of LXR, RXR and PPARM-NM-1 in mouse liver reveals extensive sharing of binding sites

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2012-01-31 | E-GEOD-35262 | biostudies-arrayexpress

Purification of Human β and γ Actin from Budding Yeast

Project description:To facilitate biochemical studies of human cytoplasmic actins, Saccharomyces cerevisiaestrains were developed that express either human β-actin or γ-actin as their sole actin. Actins purified from these strains have biochemical properties similar to mammalian skeletal muscle α-actin, but display differential binding to some key actin regulators. Mass-spectrometry analysis shows that the human actins made from yeast generally retain their N-terminal methionines, which are modified by acetylation.

2023-04-24 | PXD040174 | Pride

Modulation of NKG2D ligand expression and metastasis in tumors by spironolactone via RXR-gamma activation

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Modulation of NKG2D ligand expression and metastasis in tumors by spironolactone via RXR-gamma activation

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Molecular determinant for MED1 interaction with the VDR-RXR heterodimer

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Retinoid X receptor gamma signaling accelerates CNS remyelination

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