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Relevant bibliographies by topics / Groucho/TLE

Academic literature on the topic 'Groucho/TLE'

Author: Grafiati

Published: 11 March 2023

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Journal articles on the topic "Groucho/TLE"

1

Desjobert, Cecile, Peter Noy, Tracey Swingler, Hannah Williams, Kevin Gaston, and Padma-Sheela Jayaraman. "The PRH/Hex repressor protein causes nuclear retention of Groucho/TLE co-repressors." Biochemical Journal 417, no. 1 (December 12, 2008): 121–32. http://dx.doi.org/10.1042/bj20080872.

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The PRH (proline-rich homeodomain) [also known as Hex (haematopoietically expressed homeobox)] protein is a transcription factor that functions as an important regulator of vertebrate development and many other processes in the adult including haematopoiesis. The Groucho/TLE (transducin-like enhancer) family of co-repressor proteins also regulate development and modulate the activity of many DNA-binding transcription factors during a range of diverse cellular processes including haematopoiesis. We have shown previously that PRH is a repressor of transcription in haematopoietic cells and that an Eh-1 (Engrailed homology) motif present within the N-terminal transcription repression domain of PRH mediates binding to Groucho/TLE proteins and enables co-repression. In the present study we demonstrate that PRH regulates the nuclear retention of TLE proteins during cellular fractionation. We show that transcriptional repression and the nuclear retention of TLE proteins requires PRH to bind to both TLE and DNA. In addition, we characterize a trans-dominant-negative PRH protein that inhibits wild-type PRH activity by sequestering TLE proteins to specific subnuclear domains. These results demonstrate that transcriptional repression by PRH is dependent on TLE availability and suggest that subnuclear localization of TLE plays an important role in transcriptional repression by PRH.

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2

Chen, Guoqing, and Albert J. Courey. "Groucho/TLE family proteins and transcriptional repression." Gene 249, no. 1-2 (May 2000): 1–16. http://dx.doi.org/10.1016/s0378-1119(00)00161-x.

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3

HUSAIN, Junaid, Rita LO, Diane GRBAVEC, and Stefano STIFANI. "Affinity for the nuclear compartment and expression during cell differentiation implicate phosphorylated Groucho/TLE1 forms of higher molecular mass in nuclear functions." Biochemical Journal 317, no. 2 (July 15, 1996): 523–31. http://dx.doi.org/10.1042/bj3170523.

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The Drosophila protein Groucho is involved in embryonic segmentation and neural development, and is implicated in the Notch signal transduction pathway. We are investigating the molecular mechanisms underlying the function of Groucho and of its mammalian homologues, the TLE (‘transducin-like Enhancer of split’) proteins. We show that Groucho/TLE1 proteins are phosphorylated. We also show that two populations of phosphorylated Groucho proteins can be identified based on their interaction with the nuclear compartment. More slowly migrating proteins with an apparent molecular mass of roughly 110 kDa interact strongly with the nuclei, while faster migrating proteins displaying molecular masses of roughly 84–85 kDa show lower affinity for the nuclear compartment. Similarly, TLE1 proteins with an apparent molecular mass of roughly 118 kDa exhibit higher affinity for the nuclear compartment than do faster migrating forms with apparent molecular masses of 90–93 kDa. Moreover, we show that the nuclear, more slowly migrating, TLE1 proteins are induced during neural determination of P19 embryonic carcinoma cells. These results implicate phosphorylation in the activity of Groucho/TLE1 proteins and suggest that phosphorylated forms of higher molecular mass are involved in nuclear functions. Finally, we show that different TLE proteins respond in different ways to the neural commitment of P19 cells, suggesting that individual members of this protein family may have non-redundant functions.

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4

Heimbucher, Thomas, Christina Murko, Baubak Bajoghli, Narges Aghaallaei, Anja Huber, Ronald Stebegg, Dirk Eberhard, Maria Fink, Antonio Simeone, and Thomas Czerny. "Gbx2 and Otx2 Interact with the WD40 Domain of Groucho/Tle Corepressors." Molecular and Cellular Biology 27, no. 1 (October 23, 2006): 340–51. http://dx.doi.org/10.1128/mcb.00811-06.

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ABSTRACT One of the earliest organizational decisions in the development of the vertebrate brain is the division of the neural plate into Otx2-positive anterior and Gbx2-positive posterior territories. At the junction of these two expression domains, a local signaling center is formed, known as the midbrain-hindbrain boundary (MHB). This tissue coordinates or “organizes” the development of neighboring brain structures, such as the midbrain and cerebellum. Correct positioning of the MHB is thought to depend on mutual repression involving these two homeobox genes. Using a cell culture colocalization assay and coimmunoprecipitation experiments, we show that engrailed homology region 1 (eh1)-like motifs of both transcription factors physically interact with the WD40 domain of Groucho/Tle corepressor proteins. In addition, heat shock-induced expression of wild-type and mutant Otx2 and Gbx2 in medaka embryos demonstrates that Groucho is required for the repression of Otx2 by Gbx2. On the other hand, the repressive functions of Otx2 on Gbx2 do not appear to be dependent on corepressor interaction. Interestingly, the association of Groucho with Otx2 is also required for the repression of Fgf8 in the MHB. Therefore Groucho/Tle family members appear to regulate key aspects in the MHB development of the vertebrate brain.

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5

GRBAVEC, Diane, Rita LO, Yanling LIU, Andy GREENFIELD, and Stefano STIFANI. "Groucho/transducin-like Enhancer of split (TLE) family members interact with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related proteins: implications for evolutionary conservation of transcription repression mechanisms." Biochemical Journal 337, no. 1 (December 17, 1998): 13–17. http://dx.doi.org/10.1042/bj3370013.

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The yeast proteins TUP1 and SSN6 form a transcription repressor complex that is recruited to different promoters via pathway-specific DNA-binding proteins and regulates the expression of a variety of genes. TUP1 is functionally related to invertebrate and vertebrate transcriptional repressors of the Groucho/transducin-like Enhancer of split (TLE) family. The aim was to examine whether similar mechanisms underlie the transcription repression functions of TUP1 and Groucho/TLEs by determining whether TLE family members can interact with yeast SSN6 and mammalian SSN6-like proteins. It is shown in the present work that SSN6 binds to TLE1 and mediates transcriptional repression when expressed in mammalian cells. Moreover, TLE1 and TLE2 interact with two mammalian proteins related to SSN6, designated as the products of the ubiquitously transcribed tetratricopeptide-repeat genes on the Y (or X) chromosomes (UTY/X). These findings suggest that mammalian TLE and UTY/X proteins may mediate repression mechanisms similar to those performed by TUP1–SSN6 in yeast.

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6

Hoffman, Brad G., Bogard Zavaglia, Mike Beach, and Cheryl D. Helgason. "Expression of Groucho/TLE proteins during pancreas development." BMC Developmental Biology 8, no. 1 (2008): 81. http://dx.doi.org/10.1186/1471-213x-8-81.

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7

Cinnamon, Einat, and Ze’ev Paroush. "Context-dependent regulation of Groucho/TLE-mediated repression." Current Opinion in Genetics & Development 18, no. 5 (October 2008): 435–40. http://dx.doi.org/10.1016/j.gde.2008.07.010.

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8

Fisher, A. L., S. Ohsako, and M. Caudy. "The WRPW motif of the hairy-related basic helix-loop-helix repressor proteins acts as a 4-amino-acid transcription repression and protein-protein interaction domain." Molecular and Cellular Biology 16, no. 6 (June 1996): 2670–77. http://dx.doi.org/10.1128/mcb.16.6.2670.

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Hairy-related proteins include the Drosophila Hairy and Enhancer of Split proteins and mammalian Hes proteins. These proteins are basic helix-loop-helix (bHLH) transcriptional repressors that control cell fate decisions such as neurogenesis or myogenesis in both Drosophila melanogaster and mammals. Hairy-related proteins are site-specific DNA-binding proteins defined by the presence of both a repressor-specific bHLH DNA binding domain and a carboxyl-terminal WRPW (Trp-Arg-Pro-Trp) motif. These proteins act as repressors by binding to DNA sites in target gene promoters and not by interfering with activator proteins, indicating that these proteins are active repressors which should therefore have specific repression domains. Here we show the WRPW motif to be a functional transcriptional repression domain sufficient to confer active repression to Hairy-related proteins or a heterologous DNA-binding protein, Ga14. This motif was previously shown to be necessary for interactions with Groucho, a genetically defined corepressor for Drosophila Hairy-related proteins. Here we show that the WRPW motif is sufficient to recruit Groucho or the TLE mammalian homologs to target gene promoters. We also show that Groucho and TLE proteins actively repress transcription when directly bound to a target gene promoter and identify a novel, highly conserved transcriptional repression domain in these proteins. These results directly demonstrate that Groucho family proteins are active transcriptional corepressors for Hairy-related proteins and are recruited by the 4-amino acid protein-protein interaction domain, WRPW.

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9

Jennings, Barbara H., and David Ish-Horowicz. "The Groucho/TLE/Grg family of transcriptional co-repressors." Genome Biology 9, no. 1 (2008): 205. http://dx.doi.org/10.1186/gb-2008-9-1-205.

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10

Patel, Sanjeevkumar R., Samina S. Bhumbra, Raghavendra S. Paknikar, and Gregory R. Dressler. "Epigenetic Mechanisms of Groucho/Grg/TLE Mediated Transcriptional Repression." Molecular Cell 45, no. 2 (January 2012): 185–95. http://dx.doi.org/10.1016/j.molcel.2011.11.007.

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Dissertations / Theses on the topic "Groucho/TLE"

1

Grbavec, Diane C. "Characterization of molecular mechanisms involving the transcriptional repression functions of mammalian Groucho/TLE proteins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0035/NQ64564.pdf.

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2

Almqvist, Jenny. "Epstein-Barr virus nuclear antigen 1, Oct & Groucho/TLE in control of promoter regulation /." Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-523-2/.

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3

Perin, Alessandro. "Controllo del self-renewal e della tumorigenicità delle glioblastoma “stem-like” cells ad opera di FOXG1." Doctoral thesis, Università degli studi di Trieste, 2012. http://hdl.handle.net/10077/7398.

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2010/2011
Glioblastoma (GBM) is the most common and malignant primary brain tumour. GBM prognosis remains dismal despite available treatments, be- cause of tumour recurrence. According to the "Glioma Stem-like Cell" (GSC) hypothesis, GBM recurrence is sustained by a fraction of cells that share similarities with normal Neural Stem Cells / Neural Precursors (NSCs). In potential agreement with this possibility, primary cell cultures with characteristics of GSCs can be established from GBM. These cells display typical hallmarks of NSCs, namely unlimited self-renewal and ability to differentiate into different neural lineages in vitro. Most importantly, GSCs are highly tumorigenic when transplanted intracranially in vivo and their in vitro self-renewal potential correlates positively with tumorigenicity and negatively with prognosis in Glioma patients. We hypothesize that the tumour-forming potential of GSCs may result from the deregulation of molecular mechanisms normally involved in NSC self-renewal, proliferation and/or differentiation. In this regard, the fork-head transcription factor, FOXG1, promotes the self-renewal of both embryonic and adult NSCs. Here we show that FOXG1 mRNA and protein are up-regulated in human Gliomas and that elevated FOXG1 expression is a bad prognostic factor in GBM patients. We show further that FOXG1 is expressed in a sub-population of GBM cells with NSC-like characteristics, as well as in cultured GSCs. More importantly, knockdown of FOXG1 significantly decreases GSC self-renewal, with a concomitant increase of the cell-cycle inhibitor, p21Cip1. We also show that FOXG1 is co-expressed in GBM and GSCs with the transcriptional co-repressor TLE, a protein known to work together with FOXG1 during forebrain development. The effect of FOXG1 knockdown on GSC self-renewal is phenocopied by TLE knockdown, as well as by the forced over-expression of the previously characterized TLE:FOXG1 antagonist, GRG6, a protein with little or no expression in GBM. More importantly, mouse orthotopic implantations of human GSCs, which were either silenced for FOXG1 or over-expressing GRG6, gave rise to smaller tumours when compared to control condition; this tumor size reduction resulted in prolonged mice survival. Together, these results suggest that FOXG1 and TLE are important regulators of GBM tumorigenesis.
XXIV Ciclo
1977

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