The mammalian transcriptional repressor RBP (CBF1) targets TFIID and TFIIA to prevent activated transcription

Olave, Ivan; Reinberg, Danny; Vales, L D

doi:10.1101/gad.12.11.1621

Cited by 82 publications

(60 citation statements)

References 66 publications

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“…The mechanism(s) underlying transcriptional repression mediated by CTIP1 in mammalian cells is unknown but may involve interaction with and disruption of the function of the general transcription machinery (48,49), interaction with chromatin components, or remodeling factors resulting in stabilization of inactive chromatin structure (50), titration of transcriptional coactivators such as p300 and CBP (46), interaction with general corepressor proteins such as Groucho (51) or CtBP2 (52), recruitment of general repressors such as NC2 (53), inhibition of the assembly of the transcriptional preinitiation complex through interaction with TATA binding protein (reviewed in Ref. 54), and/or a novel mechanism.…”

Section: Discussionmentioning

confidence: 99%

Isolation of a Novel Family of C2H2 Zinc Finger Proteins Implicated in Transcriptional Repression Mediated by Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF) Orphan Nuclear Receptors

Avram¹,

Fields²,

Top³

et al. 2000

Journal of Biological Chemistry

187

205

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Two novel and related C 2 H 2 zinc finger proteins that are highly expressed in the brain, CTIP1 and CTIP2 (COUP TF-interacting proteins 1 and 2, respectively), were isolated and shown to interact with all members of the chicken ovalbumin upstream promoter transcription factor (COUP-TF) subfamily of orphan nuclear receptors. The interaction of CTIP1 with ARP1 was studied in detail, and CTIP1 was found to harbor two independent ARP1 interaction domains, ID1 and ID2, whereas the putative AF-2 of ARP1 was required for interaction with CTIP1. CTIP1, which exhibited a punctate staining pattern within the nucleus of transfected cells, recruited cotransfected ARP1 to these foci and potentiated ARP1-mediated transcriptional repression of a reporter construct. However, transcriptional repression mediated by ARP1 acting through CTIP1 did not appear to involve recruitment of a trichostatin A-sensitive histone deacetylase(s) to the template, suggesting that this repression pathway may be distinct from that utilized by several other nuclear receptors.COUP-TFI, 1 ARP1/COUP-TFII, and Ear2/COUP-TFIII have been grouped in the same subfamily of orphan nuclear receptors based on sequence similarity (1-3), evolutionary analysis (4), and a common capacity to repress ligand-dependent transcriptional activation of target genes mediated by other nuclear receptors, such as retinoic acid (5-10), thyroid hormone (8), estrogen (11)(12)(13)(14), and vitamin D 3 (9) receptors as well as peroxisome proliferator-activated receptor α (PPARα;Ref. 15).COUP-TFs play important roles in pattern formation in the developing nervous systems of Xenopus (16) and Drosophila (17). Deletion of the COUP-TFI gene in the mouse results in * This work was supported in part by American Heart Association Grant 9640219N; NIEHS, National Institutes of Health, Grants ES00210 and ES00040; the Oregon State University College of Pharmacy; and the Laboratory of Molecular Pharmacology. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.© 2000 by The American Society for Biochemistry and Molecular Biology, Inc. ∥ An established investigator of the American Heart Association. To whom correspondence and reprint requests should be addressed: MATERIALS AND METHODS Yeast Two-hybrid Screening and cDNA CloningYeast two-hybrid screening was conducted as described previously (21) using the hinge region and putative ligand binding domain of ARP1 (amino acids 144-414) as a bait. Fragments corresponding to CTIP1 and CTIP2 (see Fig. 1A) were used to screen mouse cDNA libraries obtained from CLON-TECH and from Dr. René Hen (Columbia University), yielding several overlapping clones. These overlapping clones were then used to prepare a full-length CTIP1 construct that was inserted into the eukaryotic expression vector, pCDNA3+ (Invitrogen). Yeast β-Galactosidase Assays and GST Pull-down ExperimentsProtein-p...

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Section: Discussionmentioning

confidence: 99%

Isolation of a Novel Family of C2H2 Zinc Finger Proteins Implicated in Transcriptional Repression Mediated by Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF) Orphan Nuclear Receptors

Avram¹,

Fields²,

Top³

et al. 2000

Journal of Biological Chemistry

187

205

View full text Add to dashboard Cite

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“…Transcriptional repression seems to be mediated by different mechanisms. Based on biochemical experiments, it was proposed that RBP-J can interact directly with TFIID, a general transcription factor [33] or that RBP-J can recruit histone deacetylase-containing complexes. Previously, at least three different interactions between RBP-J and corepressor complexes have been described: a complex containing SMRT/mSin3A/ HDAC-1 (SMRT, Silencing Mediator for Retinoic acid and Thyroid hormone receptor; HDAC-1, histone deacetylase-1) or NCor/mSin3A/HDAC-1 complex [34] and a CIR/SAP30/HDAC-2 complex [35].…”

Section: Notch Target Genesmentioning

confidence: 99%

The Notch signaling pathway: Transcriptional regulation at Notch target genes

Borggrefe

Oswald

2009

Cell. Mol. Life Sci.

586

499

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. The Notch gene encodes a transmembrane receptor that gave the name to the evolutionary highly conserved Notch signaling cascade. It plays a pivotal role in the regulation of many fundamental cellular processes such as proliferation, stem cell maintenance and differentiation during embryonic and adult development. After specific ligand binding, the intracellular part of the Notch receptor is cleaved off and translocates to the nucleus, where it binds to the transcription factor RBP-J. In the absence of activated Notch, RBP-J represses Notch target genes by recruiting a corepressor complex. Here, we review Notch signaling with a focus on gene regulatory events at Notch target genes. This is of utmost importance to understand Notch signaling since certain RBP-J associated cofactors and particular epigenetic marks determine the specificity of Notch target gene expression in different cell types. We subsequently summarize the current knowledge about Notch target genes and the physiological significance of Notch signaling in development and cancer.

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“…Even-skipped (Li and Manley, 1998), MOT1 (Auble and Hahn, 1993;Auble et al, 1994Auble et al, , 1997 and Dr1 (Han and Manley, 1993;Yeung et al, 1994) are examples of repressor proteins that interact with TBP, while KruÈ ppel and Engrailed (Zuo et al, 1991;Han and Manley, 1993;Licht et al, 1993) interact with TFIIE. RBP is a cellular repressor with speci®c DNA-binding activity which, in addition, contacts two coactivators (TAFII110 and TFIIA) and subverts activated transcription by interfering with the optimal interaction between these factors (Dou et al, 1994;Olave et al, 1998). Co-repressors are proteins that bridge repressors and their ultimate target, thereby reinforcing speci®c binding.…”

Section: Introductionmentioning

confidence: 99%

A murine ATFa-associated factor with transcriptional repressing activity

et al. 2000

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The ATFa proteins, which are members of the CREB/ ATF family of transcription factors, have previously been shown to interact with the adenovirus E1a oncoprotein and to mediate its transcriptional activity; they heterodimerize with Jun, Fos or related transcription factors, possibly altering their DNA-binding speci®city; they also stably bind JNK2, a stress-induced protein kinase. Here we report the identi®cation and characterization of a novel protein isolated in a yeast two-hybrid screen using the N-terminal half of ATFa as a bait. This 1306-residue protein (mAM, for mouse ATFa-associated Modulator) is rather acidic (pHi 4.5) and contains high proportions of Ser/Thr (21%) and Pro (11%) residues. It colocalizes and interacts with ATFa in mammalian cells, contains a bipartite nuclear localization signal and possesses an ATPase activity. Transfection experiments show that mAM is able to downregulate transcriptional activity, in an ATPase-independent manner. Our results indicate that mAM interacts with several components of the basal transcription machinery (TFIIE and TFIIH), including RNAPII itself. Together, these ®ndings suggest that mAM may be involved in the ®ne-tuning of ATFaregulated gene expression, by interfering with the assembly or stability of speci®c preinitiation transcription complexes.

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The mammalian transcriptional repressor RBP (CBF1) targets TFIID and TFIIA to prevent activated transcription

Cited by 82 publications

References 66 publications

Isolation of a Novel Family of C2H2 Zinc Finger Proteins Implicated in Transcriptional Repression Mediated by Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF) Orphan Nuclear Receptors

Isolation of a Novel Family of C2H2 Zinc Finger Proteins Implicated in Transcriptional Repression Mediated by Chicken Ovalbumin Upstream Promoter Transcription Factor (COUP-TF) Orphan Nuclear Receptors

The Notch signaling pathway: Transcriptional regulation at Notch target genes

A murine ATFa-associated factor with transcriptional repressing activity

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