Mouse steroid receptor coactivator-1 is not essential for peroxisome proliferator-activated receptor α-regulated gene expression

Qi, Chao; Zhu, Yijun; Pan, Jie; Yeldandi, Anjana V.; Rao, M. Sambasiva; Maeda, Nobuyo; Subbarao, V.; Pulikuri, Sujata; Hashimoto, Takashi; Reddy, Janardan K.

doi:10.1073/pnas.96.4.1585

Cited by 69 publications

(70 citation statements)

References 45 publications

(63 reference statements)

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“…While mice lacking each of the p160 factors are viable, subtle defects are suggested in specific receptor functions (43)(44)(45)(46); for example, p/CIP/SRC-3 exerts effects on somatic growth, modulating cell-autonomous cell cycle events (45,46).…”

Section: Minireview: Nuclear Receptor Coregulators 36866mentioning

confidence: 99%

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Rosenfeld¹,

Glass²

2001

Journal of Biological Chemistry

467

371

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Members of the nuclear receptor superfamily directly activate or repress target genes by binding to hormone response elements (HREs) 1 in promoter or enhancer regions, and by binding to other DNA sequence-specific activators and can inhibit the transcriptional activities of other classes of transcription factors by transrepression. Hormone response elements provide specificity to receptor homodimer heterodimer binding (reviewed in Ref.2). Nuclear receptor functions are directed by specific activation domains, referred to as activation function 1 (AF-1), which resides in the N terminus, and activation function 2 (AF-2), which resides in the C-terminal ligand binding domain (LBD) (reviewed in Ref. 1). Regulation of gene transcription by nuclear receptors requires the recruitment of proteins characterized as coregulators, with liganddependent exchange of corepressors for coactivators serving as the basic mechanism for switching gene repression to activation. In this review, we discuss biochemical and genetic studies suggesting that coregulatory complexes are differentially utilized in both a cell-and promoter-specific fashion to activate or repress gene transcription. These coregulatory components, themselves targets of diverse intracellular signaling pathways, provide a combinatorial code for tissue-and gene-specific responses, utilizing both enzymatic and platform assembly functions to mediate the actions of nuclear receptor genetic programs critical for developmental and homeostatic processes in metazoan organisms. Nuclear Receptor CoactivatorsA diverse group of proteins have emerged as potential coactivators for nuclear receptors. Ligand-dependent recruitment of coactivators is dependent on AF-2, which consists of a short conserved helical sequence within the C terminus of the LBD (2). Biochemical and expression cloning approaches have been used to identify a large number of factors that interact with nuclear receptors in either a ligand-independent or a ligand-dependent manner and are often components of large multiprotein complexes. Many of these factors are capable of potentiating nuclear receptor activity in transient cotransfection assays. In addition, a distinct set of coactivators is associated with the AF-1 domain. As the number of potential coregulators clearly exceeds the capacity for direct interaction by a single receptor, the most plausible hypothesis is that transcriptional activation by nuclear receptors involves the actions of multiple factors. These factors act in a sequential and/or combinatorial manner to reorganize chromatin templates and to modify and recruit basal factors and RNA polymerase II (3, 4). ATP-dependent Chromatin Remodeling ComplexesAs chromatinized transcription units are "repressed" compared with naked DNA, a critical aspect of gene activation involves nucleosomal remodeling (reviewed in Refs. 3-5). Two general classes of chromatin remodeling factors that appear to play critical roles in transcriptional activation by nuclear receptors have been identified. These are ATP-depen...

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Section: Minireview: Nuclear Receptor Coregulators 36866mentioning

confidence: 99%

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Rosenfeld¹,

Glass²

2001

Journal of Biological Chemistry

467

371

View full text Add to dashboard Cite

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“…SRC-1 Ϫ/Ϫ mice are partially resistant to steroid and thyroid hormones and exhibit a delayed development of cerebellar Purkinje cells (9,13,14). Peroxisome proliferatoractivated receptor ␥ function is partially impaired in brown fat of SRC-1 Ϫ/Ϫ mice causing lower energy expenditure and higher sensitivity to diet-induced obesity (15,16). Unlike SRC-1 Ϫ/Ϫ mice, TIF2 Ϫ/Ϫ mice exhibit higher energy expenditure and are resistant to diet-induced obesity (16).…”

mentioning

confidence: 99%

Partially redundant functions of SRC-1 and TIF2 in postnatal survival and male reproduction

Mark

Yoshida-Komiya

Géhin

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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“…The construction and characterization of the null mice lines for SRC-1 [22], SRC-2/TIF2 [23], and SRC-3 [18] have been described. The concentration of Cyp2b10 and SRC mRNAs in wild type or individual SRC null mice was determined by both semi-quantitative and realtime quantitative RT-PCR.…”

Section: Assay Of Cyp2b10 and P160 Coactivator Mrna Levels In Src-nulmentioning

confidence: 99%

Redundant enhancement of mouse constitutive androstane receptor transactivation by p160 coactivator family members

Xia

Liao

Sarkar³

et al. 2007

Archives of Biochemistry and Biophysics

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Constitutive androstane receptor (CAR) transactivation is enhanced by p160 coactivators, which include three members, SRC-1, SRC-2, and SRC-3. Each of the p160 coactivators enhanced mouse CAR (mCAR) transactivation of the CYP2B1 phenobarbital (PB)-responsive enhancer in transfected cultured cells and mouse hepatocytes in vivo. The cellular localization of the p160 coactivators in hepatocytes in vivo was not altered by PB treatment, nor did any of the p160 coactivators selectively colocalize with mCAR in the nucleus. Exogenous expression of each p160 coactivator mediated the PB-independent nuclear accumulation of mCAR in hepatocytes in vivo. Induction of Cyp2b10 gene expression by PB was equivalent or greater in mice null for each of the p160 coactivators than in wild type mice. These results indicate that the p160 coactivators are redundant with regard to enhancing CAR-mediated induction of cytochrome P450 genes. SRC-3 alone of the p160 coactivators enhanced CAR transactivation in hepatic cells without PB treatment.

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Mouse steroid receptor coactivator-1 is not essential for peroxisome proliferator-activated receptor α-regulated gene expression

Cited by 69 publications

References 45 publications

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Partially redundant functions of SRC-1 and TIF2 in postnatal survival and male reproduction

Redundant enhancement of mouse constitutive androstane receptor transactivation by p160 coactivator family members

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