Differential Use of CREB Binding Protein-Coactivator Complexes

Kurokawa, Riki; Kalafus, Daniel; Ogliastro, Marie-Hélène; Kioussi, Chrissa; Xu, Lan; Torchia, Joseph; Rosenfeld, Michael G.; Glass, Christopher K.

doi:10.1126/science.279.5351.700

Cited by 211 publications

(179 citation statements)

References 30 publications

Supporting

Mentioning

167

Contrasting

Unclassified

Order By: Relevance

“…PRMTI, a second arginine methyltransferase related to CARM1, also functions independently as a nuclear receptor coactivator (17). The CBP/p300 coactivators can recruit additional factors with HAT activity, such as the p/CAF⅐Gcn5L complexes (11,18). The content and conformation of the recruited complexes may explain why distinct acetyltransferases are required by different DNA-bound transcription factors on specific gene targets (28).…”

Section: Nuclear Receptor-interacting Coactivatorsmentioning

confidence: 99%

“…The central conserved domain mediates ligand-dependent interactions with the nuclear receptor LBD, whereas the conserved C-terminal transcriptional activation domains mediate interactions with either CBP/p300 or protein-arginine methyltransferase (16,17). Based on the presence of three regulatory domains, members of the p160 family have been suggested to function as coactivators, at least in part, by serving as adapter molecules that recruit CBP and/or p300 complexes to promoter-bound nuclear receptors in a ligand-dependent manner (18,19). Biochemical studies have also demonstrated strong ligand-dependent interactions between nuclear receptors and p140 factors, probably representing the coregulator RIP140, which results in a reproductive defect in female mice on gene deletion (20).…”

Section: Nuclear Receptor-interacting Coactivatorsmentioning

confidence: 99%

See 1 more Smart Citation

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Rosenfeld¹,

Glass²

2001

Journal of Biological Chemistry

Self Cite

464

369

View full text Add to dashboard Cite

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...

show abstract

Section: Nuclear Receptor-interacting Coactivatorsmentioning

confidence: 99%

Section: Nuclear Receptor-interacting Coactivatorsmentioning

confidence: 99%

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Rosenfeld¹,

Glass²

2001

Journal of Biological Chemistry

Self Cite

464

369

View full text Add to dashboard Cite

show abstract

“…The same co-activator proteins target transcription factors involved in both cell proliferation such as E2F (Trouche et al, 1996) and AP-1 (Arias et al, 1994), and differentiation such as MyoD (Puri et al, 1997) and retinoic acid receptor (Kurokawa et al, 1998). The association of co-activators with either type of transcription factors can be regulated by diverse signals from mitogens or differentiation-inducing stimuli.…”

Section: Introductionmentioning

confidence: 99%

Transcriptional activation by the oestrogen receptor α is modulated through inhibition of cyclin-dependent kinases

et al. 2002

View full text Add to dashboard Cite

We have investigated the interaction between the expression of p21 WAF1/CIP1/SDI1 , a stoichiometric inhibitor of Cdk, and the transcriptional activity of the oestrogen receptor a (ERa). Transient transfection experiments demonstrated that the expression of p21 WAF1/CIP1/SDI1 amplified the transcriptional activation by ERa. A dominant negative mutant of Cdk2 also enhanced the ERa transcriptional activity, indicating that the underlying mechanism relies on the inhibition of Cdk2 activity and cell cycle arrest. In agreement with this conclusion, experiments with p21 WAF1/CIP1/SDI1 mutants demonstrated that the domain involved in the binding of p21 WAF1/CIP1/SDI1 to Cdks was indispensable for the modulation of ERa activity. In addition, we show that expression of p21 WAF1/CIP1/SDI1 alleviates the block on CBP function mediated by Cdk2 and in turn stimulates transcriptional activation by ERa in a CBPhistone acetyltransferase (HAT)-dependent manner. These results suggest a novel mechanism by which p21 WAF1/CIP1/SDI1 functions as an enhancer of ERa activity through the modulation of CBP function.

show abstract

“…Upon interaction with ligand, the receptor complex recruits coactivator proteins such as the p160 family to its C-terminal transactivating function (AF-2) domain as well as a p300 family member. This complex contains histone acetyl transferase activity which is thought to modify chromatin such that recruitment and/or stimulation of the basal transcriptional machinery is facilitated (Chen et al, 1997;Korzus et al, 1998;Kurokawa et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Ectopic expression of cyclin D1 amplifies a retinoic acid-induced mitochondrial death pathway in breast cancer cells

et al. 2001

View full text Add to dashboard Cite

All-trans retinoic acid inhibits growth associated with downregulation of cyclin D1 and can cause low level apoptosis in estrogen receptor positive breast cancer cell lines. The cyclin D1 gene is ampli®ed and/or the protein overexpressed in about one-third of breast cancers. Constitutive expression of cyclin D1 in estrogen receptor positive MCF-7 and ZR-75 breast cancer cells (MCF-7(cycD1) and ZR-75(cycD1)) Increased the fraction of cells in S phase and reduced the G1 accumulation following retinoic acid treatment compared with control cells. However, culture of MCF-7(cycD1) with 1 mM alltrans retinoic acid resulted in about threefold greater growth inhibition compared with vector-transfected cells. Hoechst staining of DNA and in situ DNA end-labeling analysis indicated that MCF-7(cycD1) and ZR-75(cycD1) cultures contained 4 ± 6-fold more retinoic acid-induced apoptotic nuclei as vector-transfected cells. Retinoic acid treatment of vector-transfected clones resulted in Bax protein activation as assessed by exposure of the NH 2 -terminus of Bax but the proportion of cells containing activated Bax was increased in cyclin D-expressing cells treated with retinoic acid. The latter cells also displayed both immunocytochemical and biochemical evidence of translocation of cytochrome c into the cytosol following RA-treatment. Retinoic acid markedly decreased the Bcl-2 levels in MCF-7 and ZR-75 cells. Accordingly, coexpression of Bcl-2 and cyclin D1 rendered the cells resistant to retinoic acid-induced apoptosis. We conclude that constitutive expression of cyclin D1 sensitizes ER-positive breast cancer cells to a retinoic acid-induced mitochondrial death pathway involving Bax activation, cytochrome c release and caspase-9 cleavage. Oncogene (2001) 20, 3506 ± 3518.

show abstract

Differential Use of CREB Binding Protein-Coactivator Complexes

Cited by 211 publications

References 30 publications

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Coregulator Codes of Transcriptional Regulation by Nuclear Receptors

Transcriptional activation by the oestrogen receptor α is modulated through inhibition of cyclin-dependent kinases

Ectopic expression of cyclin D1 amplifies a retinoic acid-induced mitochondrial death pathway in breast cancer cells

Contact Info

Product

Resources

About