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Journal articles on the topic 'Chromatin Chromatin Receptors'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Hsiao, Pei-Wen, Bonnie J. Deroo, and Trevor K. Archer. "Chromatin remodeling and tissue-selective responses of nuclear hormone receptors." Biochemistry and Cell Biology 80, no. 3 (2002): 343–51. http://dx.doi.org/10.1139/o02-082.

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Chromatin structure of eukaryotic genes regulates gene expression by controlling the accessibility of regulatory factors. To overcome the inhibitory nature of chromatin, protein complexes that modify higher order chromatin organization and histoneDNA contacts are critical players in regulating transcription. For example, nuclear hormone receptors regulate transcription by interacting with ATP-dependent chromatin-remodeling complexes and coactivators, which include histone acetyltransferases and histone methylases that modify the basic residues of histones. A growing number of tissue-specific

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2

Hebbar, Pratibha B., and Trevor K. Archer. "Chromatin remodeling by nuclear receptors." Chromosoma 111, no. 8 (2003): 495–504. http://dx.doi.org/10.1007/s00412-003-0232-x.

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3

Hsiao, Pei-Wen, Christy J. Fryer, Kevin W. Trotter, Weidong Wang, and Trevor K. Archer. "BAF60a Mediates Critical Interactions between Nuclear Receptors and the BRG1 Chromatin-Remodeling Complex for Transactivation." Molecular and Cellular Biology 23, no. 17 (2003): 6210–20. http://dx.doi.org/10.1128/mcb.23.17.6210-6220.2003.

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ABSTRACT Nuclear hormone receptors are ligand-dependent transcriptional regulators that modulate chromatin structure. However, the precise molecular mechanisms by which receptors recruit chromatin-remodeling activity are not fully elucidated. We show that in the absence of its ligand-binding domain, the glucocorticoid receptor (GR) is able to interact with both nuclear receptor coactivators and the BRG1 chromatin-remodeling complex in vivo. Individually, the GR makes direct interactions with BRG1-associated factor 60a (BAF60a) and BAF57, but not with BRG1, BAF155, or BAF170. Further, BAF60a po

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4

Acevedo, Mari Luz, and W. Lee Kraus. "Transcriptional activation by nuclear receptors." Essays in Biochemistry 40 (June 1, 2004): 73–88. http://dx.doi.org/10.1042/bse0400073.

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Transcriptional activation by nuclear receptors (NRs) involves the recruitment of distinct classes of co-activators and other transcription-related factors to target promoters in the chromatin environment of the nucleus. Chromatin has a general repressive effect on transcription, but also provides opportunities for NRs to regulate transcription by directing specific patterns of chromatin remodelling and histone modification. Ultimately, the transcription of hormone-regulated genes by NRs is critically dependent on co-ordinated physical and functional interactions among the receptors, chromatin

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5

Trotter, Kevin W., and Trevor K. Archer. "Nuclear receptors and chromatin remodeling machinery." Molecular and Cellular Endocrinology 265-266 (February 2007): 162–67. http://dx.doi.org/10.1016/j.mce.2006.12.015.

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6

Reikhardt, B. A., O. G. Kulikova, and N. S. Sapronov. "Receptors of chromatin for drug discovery." European Neuropsychopharmacology 6 (June 1996): 197–98. http://dx.doi.org/10.1016/0924-977x(96)88230-7.

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7

Liu, Jimin, and Donald B. DeFranco. "Chromatin Recycling of Glucocorticoid Receptors: Implications for Multiple Roles of Heat Shock Protein 90." Molecular Endocrinology 13, no. 3 (1999): 355–65. http://dx.doi.org/10.1210/mend.13.3.0258.

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Abstract Unliganded glucocorticoid receptors (GRs) released from chromatin after hormone withdrawal remain associated with the nucleus within a novel subnuclear compartment that serves as a nuclear export staging area. We set out to examine whether unliganded nuclear receptors cycle between distinct subnuclear compartments or require cytoplasmic transit to regain hormone and chromatin-binding capacity. Hormone-withdrawn rat GrH2 hepatoma cells were permeabilized with digitonin to deplete cytoplasmic factors, and then hormone-binding and chromatin-binding properties of the recycled nuclear GRs

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8

Gadaleta, Raffaella Maria, and Luca Magnani. "Nuclear receptors and chromatin: an inducible couple." Journal of Molecular Endocrinology 52, no. 2 (2013): R137—R149. http://dx.doi.org/10.1530/jme-13-0170.

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The nuclear receptor (NR) family comprises 48 transcription factors (TFs) with essential and diverse roles in development, metabolism and disease. Differently from other TFs, NRs engage with well-defined DNA-regulatory elements, mostly after ligand-induced structural changes. However, NR binding is not stochastic, and only a fraction of the cognate regulatory elements within the genome actively engage with NRs. In this review, we summarize recent advances in the understanding of the interactions between NRs and DNA. We discuss how chromatin accessibility and epigenetic modifications contribute

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9

Collingwood, TN, FD Urnov, and AP Wolffe. "Nuclear receptors: coactivators, corepressors and chromatin remodeling in the control of transcription." Journal of Molecular Endocrinology 23, no. 3 (1999): 255–75. http://dx.doi.org/10.1677/jme.0.0230255.

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A contemporary view of hormone action at the transcriptional level requires knowledge of the transcription factors including the hormone receptor that may bind to promoters or enhancers, together with the chromosomal context within which these regulatory proteins function. Nuclear receptors provide the best examples of transcriptional control through the targeted recruitment of large protein complexes that modify chromosomal components and reversibly stabilize or destabilize chromatin. Ligand-dependent recruitment of transcriptional coactivators destabilizes chromatin by mechanisms including h

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10

Hager, G. L., T. M. Fletcher, N. Xiao, C. T. Baumann, W. G. Müller, and J. G. McNally. "Dynamics of gene targeting and chromatin remodelling by nuclear receptors." Biochemical Society Transactions 28, no. 4 (2000): 405–10. http://dx.doi.org/10.1042/bst0280405.

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Activation of the murine-mammary-tumour virus (MMTV) promoter by the glucocorticoid receptor (GR) is associated with a chromatin structural transition in the B nucleosome region of the viral long terminal repeat (LTR). We have reconstituted this nucleoprotein transition with chromatin assembled on MMTV LTR DNA with Drosophila embryo extracts, purified GR, and HeLa nuclear extract. Chromatin remodelling in vitro is ATP-dependent and maps to a region identical with that found in vivo. We demonstrate specific, glucocorticoid response element dependent, binding of purified GR to a large, multi-nuc

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11

Vicent, Guillermo P., A. Silvina Nacht, Roser Zaurín, Cecilia Ballaré, Jaime Clausell, and Miguel Beato. "Minireview: Role of Kinases and Chromatin Remodeling in Progesterone Signaling to Chromatin." Molecular Endocrinology 24, no. 11 (2010): 2088–98. http://dx.doi.org/10.1210/me.2010-0027.

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Abstract Steroid hormones regulate gene expression by interaction of their receptors with hormone-responsive elements on DNA or with other transcription factors, but they can also activate cytoplasmic signaling cascades. Rapid activation of Erk by progestins via an interaction of the progesterone receptor (PR) with the estrogen receptor is critical for transcriptional activation of the mouse mammary tumor virus (MMTV) promoter and other progesterone target genes. Erk activation leads to the phosphorylation of PR, activation of mitogen- and stress-activated protein kinase 1, and the recruitment

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12

Xu, Wei. "Nuclear receptor coactivators: the key to unlock chromatin." Biochemistry and Cell Biology 83, no. 4 (2005): 418–28. http://dx.doi.org/10.1139/o05-057.

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The biological effects of hormones, ranging from organogenesis, metabolism, and proliferation, are transduced through nuclear receptors (NRs). Over the last decade, NRs have been used as a model to study transcriptional control. The conformation of activated NRs is favorable for the recruitment of coactivators, which promote transcriptional activation by directly communicating with chromatin. This review will focus on the function of different classes of coactivators and associated complexes, and on progress in our understanding of gene activation by NRs through chromatin remodeling.Key words:

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13

Wolffe, Alan P. "Chromatin remodeling regulated by steroid and nuclear receptors." Cell Research 7, no. 2 (1997): 127–42. http://dx.doi.org/10.1038/cr.1997.14.

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14

Paakinaho, Ville, Erin E. Swinstead, Diego M. Presman, Lars Grøntved, and Gordon L. Hager. "Meta-analysis of Chromatin Programming by Steroid Receptors." Cell Reports 28, no. 13 (2019): 3523–34. http://dx.doi.org/10.1016/j.celrep.2019.08.039.

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15

Haining, W. Nicholas. "Chromatin State and Immunotherapy." Blood 132, Supplement 1 (2018): SCI—16—SCI—16. http://dx.doi.org/10.1182/blood-2018-99-109432.

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Abstract The functional impairment of T cell-mediated immunity within the tumor microenvironment (TME) is a defining feature of many cancers. Checkpoint blockade therapy seeks to reinvigorate T cell responses by targeting inhibitory receptors such as PD-1, which are upregulated by dysfunctional TILs. However, the fundamental mechanisms underlying T cell dysfunction in the TME remain poorly understood, as are the mechanisms by which checkpoint blockade overcomes this dysfunction. Initial studies of dysfunctional CD8+ T cells in both human and mouse tumors suggested that they share features of T

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16

Aranda, Ana, and Angel Pascual. "Nuclear Hormone Receptors and Gene Expression." Physiological Reviews 81, no. 3 (2001): 1269–304. http://dx.doi.org/10.1152/physrev.2001.81.3.1269.

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The nuclear hormone receptor superfamily includes receptors for thyroid and steroid hormones, retinoids and vitamin D, as well as different “orphan” receptors of unknown ligand. Ligands for some of these receptors have been recently identified, showing that products of lipid metabolism such as fatty acids, prostaglandins, or cholesterol derivatives can regulate gene expression by binding to nuclear receptors. Nuclear receptors act as ligand-inducible transcription factors by directly interacting as monomers, homodimers, or heterodimers with the retinoid X receptor with DNA response elements of

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17

Kinyamu, H. K., J. Chen, and T. K. Archer. "Linking the ubiquitin–proteasome pathway to chromatin remodeling/modification by nuclear receptors." Journal of Molecular Endocrinology 34, no. 2 (2005): 281–97. http://dx.doi.org/10.1677/jme.1.01680.

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Over 25 years ago, eukaryotic cells were shown to contain a highly specific system for the selective degradation of short-lived proteins, this system is known as the ubiquitin–proteasome pathway. In this pathway, proteins are targeted for degradation by covalent modification by a small highly conserved protein named ubiquitin. Ubiquitin-mediated degradation of regulatory proteins plays an important role in numerous cell processes, including cell cycle progression, signal transduction and transcriptional regulation. Recent experiments have shown that the ubiquitin–proteasome pathway is also inv

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18

Guan, Wenyue, Romain Guyot, Jacques Samarut, Frédéric Flamant, Jiemin Wong, and Karine Cécile Gauthier. "Methylcytosine dioxygenase TET3 interacts with thyroid hormone nuclear receptors and stabilizes their association to chromatin." Proceedings of the National Academy of Sciences 114, no. 31 (2017): 8229–34. http://dx.doi.org/10.1073/pnas.1702192114.

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Thyroid hormone receptors (TRs) are members of the nuclear hormone receptor superfamily that act as ligand-dependent transcription factors. Here we identified the ten-eleven translocation protein 3 (TET3) as a TR interacting protein increasing cell sensitivity to T3. The interaction between TET3 and TRs is independent of TET3 catalytic activity and specifically allows the stabilization of TRs on chromatin. We provide evidence that TET3 is required for TR stability, efficient binding of target genes, and transcriptional activation. Interestingly, the differential ability of different TRα1 mutan

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19

Biddie, Simon C., and Sam John. "Minireview: Conversing With Chromatin: The Language of Nuclear Receptors." Molecular Endocrinology 28, no. 1 (2014): 3–15. http://dx.doi.org/10.1210/me.2013-1247.

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20

Lee, Kathleen C., and W. Lee Kraus. "Nuclear receptors, coactivators and chromatin: new approaches, new insights." Trends in Endocrinology & Metabolism 12, no. 5 (2001): 191–97. http://dx.doi.org/10.1016/s1043-2760(01)00392-7.

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21

Ruh, M. F., R. K. Singh, T. S. Ruh, and G. Shyamala. "Binding of glucocorticoid receptors to mammary chromatin acceptor sites." Journal of Steroid Biochemistry 28, no. 6 (1987): 581–86. http://dx.doi.org/10.1016/0022-4731(87)90383-9.

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22

Swinstead, Erin E., Tina B. Miranda, Ville Paakinaho, et al. "Steroid Receptors Reprogram FoxA1 Occupancy through Dynamic Chromatin Transitions." Cell 165, no. 3 (2016): 593–605. http://dx.doi.org/10.1016/j.cell.2016.02.067.

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23

Swinstead, Erin E., Ville Paakinaho, and Gordon L. Hager. "Chromatin reprogramming in breast cancer." Endocrine-Related Cancer 25, no. 7 (2018): R385—R404. http://dx.doi.org/10.1530/erc-18-0033.

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Reprogramming of the chromatin landscape is a critical component to the transcriptional response in breast cancer. Effects of sex hormones such as estrogens and progesterone have been well described to have a critical impact on breast cancer proliferation. However, the complex network of the chromatin landscape, enhancer regions and mode of function of steroid receptors (SRs) and other transcription factors (TFs), is an intricate web of signaling and functional processes that is still largely misunderstood at the mechanistic level. In this review, we describe what is currently known about the

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24

Kemper, Jongsook Kim, Hwajin Kim, Ji Miao, Sonali Bhalla, and Yangjin Bae. "Role of an mSin3A-Swi/Snf Chromatin Remodeling Complex in the Feedback Repression of Bile Acid Biosynthesis by SHP." Molecular and Cellular Biology 24, no. 17 (2004): 7707–19. http://dx.doi.org/10.1128/mcb.24.17.7707-7719.2004.

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ABSTRACT The orphan receptor SHP interacts with many nuclear receptors and inhibits their transcriptional activities. SHP is central to feedback repression of cholesterol 7α hydroxylase gene (CYP7A1) expression by bile acids, which is critical for maintaining cholesterol homeostasis. Using CYP7A1 as a model system, we studied the molecular mechanisms of SHP repression at the level of native chromatin. Chromatin immunoprecipitation studies showed that mSin3A and a Swi/Snf complex containing Brm as a central ATPase were recruited to the promoter. This recruitment was associated with chromatin re

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25

Millard, Christopher J., Peter J. Watson, Louise Fairall, and John W. R. Schwabe. "An evolving understanding of nuclear receptor coregulator proteins." Journal of Molecular Endocrinology 51, no. 3 (2013): T23—T36. http://dx.doi.org/10.1530/jme-13-0227.

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Nuclear receptors are transcription factors that regulate gene expression through the ligand-controlled recruitment of a diverse group of proteins known as coregulators. Most nuclear receptor coregulators function in large multi-protein complexes that modify chromatin and thereby regulate the transcription of target genes. Structural and functional studies are beginning to reveal how these complexes are assembled bringing together multiple functionalities that mediate: recruitment to specific genomic loci through interaction with transcription factors; recruitment of enzymatic activities that

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Paakinaho, Ville, and Jorma J. Palvimo. "Genome-wide crosstalk between steroid receptors in breast and prostate cancers." Endocrine-Related Cancer 28, no. 9 (2021): R231—R250. http://dx.doi.org/10.1530/erc-21-0038.

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Steroid receptors (SRs) constitute an important class of signal-dependent transcription factors (TFs). They regulate a variety of key biological processes and are crucial drug targets in many disease states. In particular, estrogen (ER) and androgen receptors (AR) drive the development and progression of breast and prostate cancer, respectively. Thus, they represent the main specific drug targets in these diseases. Recent evidence has suggested that the crosstalk between signal-dependent TFs is an important step in the reprogramming of chromatin sites; a signal-activated TF can expand or restr

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Jahan, Sanzida, Tasnim H. Beacon, Wayne Xu, and James R. Davie. "Atypical chromatin structure of immune-related genes expressed in chicken erythrocytes." Biochemistry and Cell Biology 98, no. 2 (2020): 171–77. http://dx.doi.org/10.1139/bcb-2019-0107.

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The major biological role of red blood cells is to carry oxygen to the tissues in the body. However, another role of the erythroid cell is to participate in the immune response. Mature erythrocytes from chickens express Toll-like receptors and several cytokines in response to stimulation of the immune system. We previously reported the application of a biochemical fractionation protocol to isolate highly enriched transcribed DNA from polychromatic erythrocytes from chickens. In conjunction with next-generation DNA, RNA sequencing, chromatin immunoprecipitation-DNA sequencing, and formaldehyde-

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28

Davies, P., and N. K. Rushmere. "Association of glucocorticoid receptors with prostate nuclear sites for androgen receptors and with androgen response elements." Journal of Molecular Endocrinology 5, no. 2 (1990): 117–27. http://dx.doi.org/10.1677/jme.0.0050117.

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ABSTRACT Ventral prostate glands of intact normal rats contained low levels (2500 molecules/cell) of high-affinity (dissociation constant (Kd) 0·57 nmol/l) glucocorticoid receptors (GR). Levels of GR increased 2·8-fold 1 day after castration, and 4·3-fold 3 days after castration. Nuclear GR increased from a normal value of 1150 molecules/nucleus to 5200 molecules/nucleus 3 days after castration. The greater increase in intranuclear GR was in that associated with oligomeric chromatin. Although nuclear GR never approached the normal population of nuclear androgen receptors (AR; approximately 160

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DiRenzo, James, Yongfeng Shang, Michael Phelan, et al. "BRG-1 Is Recruited to Estrogen-Responsive Promoters and Cooperates with Factors Involved in Histone Acetylation." Molecular and Cellular Biology 20, no. 20 (2000): 7541–49. http://dx.doi.org/10.1128/mcb.20.20.7541-7549.2000.

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ABSTRACT Several factors that mediate activation by nuclear receptors also modify the chemical and structural composition of chromatin. Prominent in this diverse group is the steroid receptor coactivator 1 (SRC-1) family, which interact with agonist-bound nuclear receptors, thereby coupling them to multifunctional transcriptional coregulators such as CREB-binding protein (CBP), p300, and PCAF, all of which have potent histone acetyltransferase activity. Additionally factors including the Brahma-related gene 1 (BRG-1) that are involved in the structural remodeling of chromatin also mediate horm

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Papadopoulos, Natalia, Johan Lennartsson та Carl-Henrik Heldin. "PDGFRβ translocates to the nucleus and regulates chromatin remodeling via TATA element–modifying factor 1". Journal of Cell Biology 217, № 5 (2018): 1701–17. http://dx.doi.org/10.1083/jcb.201706118.

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Translocation of full-length or fragments of receptors to the nucleus has been reported for several tyrosine kinase receptors. In this paper, we show that a fraction of full-length cell surface platelet-derived growth factor (PDGF) receptor β (PDGFRβ) accumulates in the nucleus at the chromatin and the nuclear matrix after ligand stimulation. Nuclear translocation of PDGFRβ was dependent on PDGF-BB–induced receptor dimerization, clathrin-mediated endocytosis, β-importin, and intact Golgi, occurring in both normal and cancer cells. In the nucleus, PDGFRβ formed ligand-inducible complexes with t

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31

Abroi, Aare, Ivar Ilves, Sirje Kivi, and Mart Ustav. "Analysis of Chromatin Attachment and Partitioning Functions of Bovine Papillomavirus Type 1 E2 Protein." Journal of Virology 78, no. 4 (2004): 2100–2113. http://dx.doi.org/10.1128/jvi.78.4.2100-2113.2004.

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ABSTRACT Recent studies have suggested that the tethering of viral genomes to host cell chromosomes could provide one of the ways to achieve their nuclear retention and partitioning during extrachromosomal maintenance in dividing cells. The data we present here provide firm evidence that the partitioning of the bovine papillomavirus type 1 (BPV1) genome is dependent on the chromatin attachment process mediated by viral E2 protein and its multiple binding sites. On the other hand, the attachment of E2 and the E2-mediated tethering of reporter plasmids to host chromosomes are not necessarily suf

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32

Stender, Joshua D., Kyuri Kim, Tze Howe Charn та ін. "Genome-Wide Analysis of Estrogen Receptor α DNA Binding and Tethering Mechanisms Identifies Runx1 as a Novel Tethering Factor in Receptor-Mediated Transcriptional Activation". Molecular and Cellular Biology 30, № 16 (2010): 3943–55. http://dx.doi.org/10.1128/mcb.00118-10.

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ABSTRACT Nuclear receptor estrogen receptor alpha (ERα) controls the expression of hundreds of genes responsible for target cell phenotypic properties, but the relative importance of direct versus tethering mechanisms of DNA binding has not been established. In this first report, we examine the genome-wide chromatin localization of an altered-specificity mutant ER with a DNA binding domain deficient in binding to estrogen response element (ERE)-containing DNA (DBDmut ER) versus wild-type ERα. Using high-throughput sequencing of ER chromatin immunoprecipitations (ChIP-Seq) and mRNA transcriptio

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33

Wang, Chenguang, Michael J. Powell, Vladimir M. Popov, and Richard G. Pestell. "Acetylation in Nuclear Receptor Signaling and the Role of Sirtuins." Molecular Endocrinology 22, no. 3 (2008): 539–45. http://dx.doi.org/10.1210/me.2007-0379.

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Abstract It has been known since the early 1970s that nuclear receptor complexes bind DNA in association with coregulatory proteins. Characterization of these nuclear receptor coregulators has revealed diverse enzymatic activities that temporally and spatially coordinate nuclear receptor activity within the context of local chromatin in response to diverse hormone signals. Chromatin-modifying proteins, which dictate the higher-order chromatin structure in which DNA is packaged, in turn orchestrate orderly recruitment of nuclear receptor complexes. Modifications of histones include acetylation,

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34

Acevedo, Mari Luz, та W. Lee Kraus. "Mediator and p300/CBP-Steroid Receptor Coactivator Complexes Have Distinct Roles, but Function Synergistically, during Estrogen Receptor α-Dependent Transcription with Chromatin Templates". Molecular and Cellular Biology 23, № 1 (2003): 335–48. http://dx.doi.org/10.1128/mcb.23.1.335-348.2003.

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ABSTRACT Ligand-dependent transcriptional activation by nuclear receptors involves the recruitment of various coactivators to the promoters of hormone-regulated genes assembled into chromatin. Nuclear receptor coactivators include histone acetyltransferase complexes, such as p300/CBP-steroid receptor coactivator (SRC), as well as the multisubunit mediator complexes (“Mediator”), which may help recruit RNA polymerase II to the promoter. We have used a biochemical approach, including an in vitro chromatin assembly and transcription system, to examine the functional role for Mediator in the trans

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35

Yang, Jun, Jimin Liu, and Donald B. DeFranco. "Subnuclear Trafficking of Glucocorticoid Receptors In Vitro: Chromatin Recycling and Nuclear Export." Journal of Cell Biology 137, no. 3 (1997): 523–38. http://dx.doi.org/10.1083/jcb.137.3.523.

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We have used digitonin-permeabilized cells to examine in vitro nuclear export of glucocorticoid receptors (GRs). In situ biochemical extractions in this system revealed a distinct subnuclear compartment, which collects GRs that have been released from chromatin and serves as a nuclear export staging area. Unliganded nuclear GRs within this compartment are not restricted in their subnuclear trafficking as they have the capacity to recycle to chromatin upon rebinding hormone. Thus, GRs that release from chromatin do not require transit through the cytoplasm to regain functionality. In addition,

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36

Mitro, Nico. "Bile acids and gene regulation: from nuclear receptors to chromatin." Frontiers in Bioscience Volume, no. 13 (2008): 6276. http://dx.doi.org/10.2741/3154.

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Hager, G. L., T. M. Fletcher, N. Xiao, C. T. Baumann, W. G. Müller, and J. G. McNally. "Dynamics of gene targeting and chromatin remodelling by nuclear receptors." Biochemical Society Transactions 28, no. 4 (2000): 405. http://dx.doi.org/10.1042/0300-5127:0280405.

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Urnov, Fyodor D., and Alan P. Wolffe. "A Necessary Good: Nuclear Hormone Receptors and Their Chromatin Templates." Molecular Endocrinology 15, no. 1 (2001): 1–16. http://dx.doi.org/10.1210/mend.15.1.0589.

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39

Spelsberg, T. C., A. Goldberger, M. Horton, and J. Hora. "Nuclear acceptor sites for sex steroid hormone receptors in chromatin." Journal of Steroid Biochemistry 27, no. 1-3 (1987): 133–47. http://dx.doi.org/10.1016/0022-4731(87)90304-9.

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40

Varma, Garima, Pratishtha Rawat, Manisha Jalan, Manjula Vinayak, and Madhulika Srivastava. "Influence of a CTCF-Dependent Insulator on Multiple Aspects of Enhancer-Mediated Chromatin Organization." Molecular and Cellular Biology 35, no. 20 (2015): 3504–16. http://dx.doi.org/10.1128/mcb.00514-15.

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Developmental stage-specific enhancer-promoter-insulator interactions regulate the chromatin configuration necessary for transcription at various loci and additionally for VDJ recombination at antigen receptor loci that encode immunoglobulins and T-cell receptors. To investigate these regulatory interactions, we analyzed the epigenetic landscape of the murine T-cell receptor β (TCRβ) locus in the presence and absence of an ectopic CTCF-dependent enhancer-blocking insulator, H19-ICR, in genetically manipulated mice. Our analysis demonstrated the ability of the H19-ICR insulator to restrict seve

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Scotet, Emmanuel, Susanne Schroeder, and Antonio Lanzavecchia. "Molecular regulation of CC-chemokine receptor 3 expression in human T helper 2 cells." Blood 98, no. 8 (2001): 2568–70. http://dx.doi.org/10.1182/blood.v98.8.2568.

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Abstract In developing T helper 1 (Th1) and Th2 cells the acquisition of effector function is intimately connected with the acquisition of new migratory capacities, as exemplified by differential expression of chemokine receptors. This study investigates the molecular mechanisms responsible for Th2-restricted expression of the CC-chemokine receptor 3 (CCR3). The minimal promoter in T cells was identified in the −149 base pair (bp) upstream sequence that contains a positive regulatory element. A strong negative element was also localized in the flanking intronic sequence. The study further inve

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Brinkley, B. R., D. He, C. Zeng, B. Scott, and D. Turner. "Nucleoskeltal proteins with bifunctional roles in the nucleus and mitotic apparatus: a paradigm for protein dynamics in the cell cycle." Proceedings, annual meeting, Electron Microscopy Society of America 53 (August 13, 1995): 770–71. http://dx.doi.org/10.1017/s0424820100140221.

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The eukaryotic cell nucleus, once believed to contain structureless nucleoplasm surrounding chromatin and the nucleolus is now thought to contain an extensive nucleoskeletal matrix on which chromatin, RNP and a complex array of transcription factors, hormone receptors and other regulatory factors are spatially arranged. A distinct nucleoskeleton has been difficult to identify in the intact nucleus, due in part to masking by a dense array of chromatin fibers. However, if chromatin is extracted by nuclease digestion and high salt, an underlying anastomosing network of 9-13 nm core filaments can

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Kovács, Tamás, Edina Szabó-Meleg, and István M. Ábrahám. "Estradiol-Induced Epigenetically Mediated Mechanisms and Regulation of Gene Expression." International Journal of Molecular Sciences 21, no. 9 (2020): 3177. http://dx.doi.org/10.3390/ijms21093177.

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Gonadal hormone 17β-estradiol (E2) and its receptors are key regulators of gene transcription by binding to estrogen responsive elements in the genome. Besides the classical genomic action, E2 regulates gene transcription via the modification of epigenetic marks on DNA and histone proteins. Depending on the reaction partner, liganded estrogen receptor (ER) promotes DNA methylation at the promoter or enhancer regions. In addition, ERs are important regulators of passive and active DNA demethylation. Furthermore, ERs cooperating with different histone modifying enzymes and chromatin remodeling c

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Moehren, Udo, Maren Eckey, and Aria Baniahmad. "Gene repression by nuclear hormone receptors." Essays in Biochemistry 40 (June 1, 2004): 89–104. http://dx.doi.org/10.1042/bse0400089.

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Repression by nuclear hormone receptors (NHRs) plays an important role in development, immune response and cellular function. We review mechanisms of how NHRs act as repressors of gene transcription either by direct contact with basal transcription factors or through recruitment of cofactors and enzymic activities that modulate chromatin accessibility. We describe also the role and biochemical mechanism of the cognate hormone that switches a NHR from a transcriptional silencer into an activator. This includes data from crystal structure, functional receptor domain analyses and the role of co-r

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Bonthuis, Paul J., James K. Patteson та Emilie F. Rissman. "Acquisition of Sexual Receptivity: Roles of Chromatin Acetylation, Estrogen Receptor-α, and Ovarian Hormones". Endocrinology 152, № 8 (2011): 3172–81. http://dx.doi.org/10.1210/en.2010-1001.

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Sexually naïve, hormone-primed, C57BL/6J female mice are not receptive to mating attempts by conspecific males. Repeated experience with sexually active males and concurrent treatment with estradiol and progesterone gradually increases female receptivity over the course of five trials to maximal levels. Ovarian hormones activate their cognate nuclear steroid receptors estrogen receptor-α and progesterone receptor to induce female sexual receptivity. Nuclear receptors recruit coactivators of transcription that include histone acetyltransferases to hormone responsive genes. In this set of studie

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Deroo, Bonnie J., Claudia Rentsch, Sowmini Sampath, Janel Young, Donald B. DeFranco, and Trevor K. Archer. "Proteasomal Inhibition Enhances Glucocorticoid Receptor Transactivation and Alters Its Subnuclear Trafficking." Molecular and Cellular Biology 22, no. 12 (2002): 4113–23. http://dx.doi.org/10.1128/mcb.22.12.4113-4123.2002.

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ABSTRACT The ubiquitin-proteasome pathway regulates the turnover of many transcription factors, including steroid hormone receptors such as the estrogen receptor and progesterone receptor. For these receptors, proteasome inhibition interferes with steroid-mediated transcription. We show here that proteasome inhibition with MG132 results in increased accumulation of the glucocorticoid receptor (GR), confirming that it is likewise a substrate for the ubiquitin-proteasome degradative pathway. Using the mouse mammary tumor virus (MMTV) promoter integrated into tissue culture cells, we found that p

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Mert, Ufuk, Alshaimaa Adawy, Elisabeth Scharff, et al. "TRAIL Induces Nuclear Translocation and Chromatin Localization of TRAIL Death Receptors." Cancers 11, no. 8 (2019): 1167. http://dx.doi.org/10.3390/cancers11081167.

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Binding of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) to the plasma membrane TRAIL-R1/-R2 selectively kills tumor cells. This discovery led to evaluation of TRAIL-R1/-R2 as targets for anti-cancer therapy, yet the corresponding clinical trials were disappointing. Meanwhile, it emerged that many cancer cells are TRAIL-resistant and that TRAIL-R1/-R2-triggering may lead to tumor-promoting effects. Intriguingly, recent studies uncovered specific functions of long ignored intracellular TRAIL-R1/-R2, with tumor-promoting functions of nuclear (n)TRAIL-R2 as the regulator of let-

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KATO, Shigeaki, and Ryoji FUJIKI. "Transcriptional Controls by Nuclear Fat-Soluble Vitamin Receptors through Chromatin Reorganization." Bioscience, Biotechnology, and Biochemistry 75, no. 10 (2011): 2011E3. http://dx.doi.org/10.1271/bbb.2011e3.

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Beato, Miguel, Reyes Candau, Sebastián Chávez, Christian Möws, and Mathias Truss. "Interaction of steroid hormone receptors with transcription factors involves chromatin remodelling." Journal of Steroid Biochemistry and Molecular Biology 56, no. 1-6 (1996): 47–59. http://dx.doi.org/10.1016/0960-0760(95)00223-5.

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Urnov, Fyodor D. "A feel for the template: zinc finger protein transcription factors and chromatin." Biochemistry and Cell Biology 80, no. 3 (2002): 321–33. http://dx.doi.org/10.1139/o02-084.

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Transcription factors and chromatin collaborate in bringing the eukaryotic genome to life. An important, and poorly understood, aspect of this collaboration involves targeting the regulators to correct binding sites in vivo. An implicit and insufficiently tested assumption in the field has been that chromatin simply obstructs most sites and leaves only a few functionally relevant ones accessible. The major class of transcription factors in all metazoa, zinc finger proteins (ZFPs), can bind to chromatin in vitro (as clearly shown for Sp1, GATA-1 and -4, and the nuclear hormone receptors, for ex

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