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Journal articles on the topic 'Cytoplasmic and Nuclear Transcription'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

Billin, Andrew N., Alanna L. Eilers, Kathryn L. Coulter, Jennifer S. Logan, and Donald E. Ayer. "MondoA, a Novel Basic Helix-Loop-Helix–Leucine Zipper Transcriptional Activator That Constitutes a Positive Branch of a Max-Like Network." Molecular and Cellular Biology 20, no. 23 (2000): 8845–54. http://dx.doi.org/10.1128/mcb.20.23.8845-8854.2000.

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ABSTRACT Max is a common dimerization partner for a family of transcription factors (Myc, Mad [or Mxi]), and Mnt [or Rox] proteins) that regulate cell growth, proliferation, and apoptosis. We recently characterized a novel Max-like protein, Mlx, which interacts with Mad1 and Mad4. Here we describe the cloning and functional characterization of a new family of basic helix-loop-helix–leucine zipper heterodimeric partners for Mlx termed the Mondo family. MondoA forms homodimers weakly and does not interact with Max or members of the Myc or Mad families. MondoA and Mlx associate in vivo, and surpr

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Tolwinski, Nicholas S., and Eric Wieschaus. "Armadillo nuclear import is regulated by cytoplasmic anchor Axin and nuclear anchor dTCF/Pan." Development 128, no. 11 (2001): 2107–17. http://dx.doi.org/10.1242/dev.128.11.2107.

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Drosophila melanogaster Armadillo plays two distinct roles during development. It is a component of adherens junctions, and functions as a transcriptional activator in response to Wingless signaling. In the current model, Wingless signal causes stabilization of cytoplasmic Armadillo allowing it to enter the nucleus where it can activate transcription. However, the mechanism of nuclear import and export remains to be elucidated. In this study, we show that two gain-of-function alleles of Armadillo activate Wingless signaling by different mechanisms. The S10 allele was previously found to locali

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3

Oh, Jaewook, and Steven S. Broyles. "Host Cell Nuclear Proteins Are Recruited to Cytoplasmic Vaccinia Virus Replication Complexes." Journal of Virology 79, no. 20 (2005): 12852–60. http://dx.doi.org/10.1128/jvi.79.20.12852-12860.2005.

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ABSTRACT The initiation and termination of vaccinia virus postreplicative transcription have been reported to require cellular proteins, some of which are believed to be nuclear proteins. Vaccinia virus replicates in the cytoplasmic compartment of the cell, raising questions as to whether vaccinia virus has access to nuclear proteins. This was addressed here by following the fate of several nuclear proteins after infection of cells with vaccinia virus. The nuclear transcription factors YY1, SP1, and TATA binding protein were found to colocalize with virus replication complexes in the cytoplasm

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4

Grunau, Christoph, Susanne Voigt, Ralph Dobler, Damian Dowling, and Klaus Reinhardt. "The Cytoplasm Affects the Epigenome in Drosophila melanogaster." Epigenomes 2, no. 3 (2018): 17. http://dx.doi.org/10.3390/epigenomes2030017.

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Cytoplasmic components and their interactions with the nuclear genome may mediate patterns of phenotypic expression to form a joint inheritance system. However, proximate mechanisms underpinning these interactions remain elusive. To independently assess nuclear genetic and epigenetic cytoplasmic effects, we created a full-factorial design in which representative cytoplasms and nuclear backgrounds from each of two geographically disjunct populations of Drosophila melanogaster were matched together in all four possible combinations. To capture slowly-accumulating epimutations in addition to imme

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5

Tam, Winnie F., Linda H. Lee, Laura Davis та Ranjan Sen. "Cytoplasmic Sequestration of Rel Proteins by IκBα Requires CRM1-Dependent Nuclear Export". Molecular and Cellular Biology 20, № 6 (2000): 2269–84. http://dx.doi.org/10.1128/mcb.20.6.2269-2284.2000.

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ABSTRACT Rel and IκB protein families form a complex cellular regulatory network. A major regulatory function of IκB proteins is to retain Rel proteins in the cell cytoplasm. In addition, IκB proteins have also been postulated to serve nuclear functions. These include the maintenance of inducible NF-κB-dependent gene transcription, as well as termination of inducible transcription. We show that IκBα shuttles between the nucleus and the cytoplasm, utilizing the nuclear export receptor CRM1. A CRM1-binding export sequence was identified in the N-terminal domain of IκBα but not in that of IκBβ or

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6

McGrath, James, and Davor Solter. "Nucleocytoplasmic interactions in the mouse embryo." Development 97, Supplement (1986): 277–89. http://dx.doi.org/10.1242/dev.97.supplement.277.

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Fertilized mammalian ova consist of haploid genomes derived from both parents and cytoplasmic components inherited largely from the female parent. These three cellular compartments must successfully interact with each other and with their environment for development to proceed. These interactions require the transposition of nuclear and cytoplasmic products between cellular compartments with resultant alteration of gene transcription and the cytoplasmic expression of preformed or newly synthesized gene products. We have investigated nuclear/cytoplasmic interactions in the mouse embryo via the

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7

Wimmer, Robert J., Yewei Liu, Tova Neustadt Schachter, David P. Stonko, Bradford E. Peercy, and Martin F. Schneider. "Mathematical modeling reveals modulation of both nuclear influx and efflux of Foxo1 by the IGF-I/PI3K/Akt pathway in skeletal muscle fibers." American Journal of Physiology-Cell Physiology 306, no. 6 (2014): C570—C584. http://dx.doi.org/10.1152/ajpcell.00338.2013.

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Foxo family transcription factors contribute to muscle atrophy by promoting transcription of the ubiquitin ligases muscle-specific RING finger protein and muscle atrophy F-box/atrogin-1. Foxo transcriptional effectiveness is largely determined by its nuclear-cytoplasmic distribution, with unphosphorylated Foxo1 transported into nuclei and phosphorylated Foxo1 transported out of nuclei. We expressed the fluorescent fusion protein Foxo1-green fluorescent protein (GFP) in cultured adult mouse flexor digitorum brevis muscle fibers and tracked the time course of the nuclear-to-cytoplasmic Foxo1-GFP

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8

Laribee, R. Nicholas, and Ronit Weisman. "Nuclear Functions of TOR: Impact on Transcription and the Epigenome." Genes 11, no. 6 (2020): 641. http://dx.doi.org/10.3390/genes11060641.

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The target of rapamycin (TOR) protein kinase is at the core of growth factor- and nutrient-dependent signaling pathways that are well-known for their regulation of metabolism, growth, and proliferation. However, TOR is also involved in the regulation of gene expression, genomic and epigenomic stability. TOR affects nuclear functions indirectly through its activity in the cytoplasm, but also directly through active nuclear TOR pools. The mechanisms by which TOR regulates its nuclear functions are less well-understood compared with its cytoplasmic activities. TOR is an important pharmacological

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9

Kumar, K. Prasanna, Kevin M. McBride, Brian K. Weaver, Colin Dingwall, and Nancy C. Reich. "Regulated Nuclear-Cytoplasmic Localization of Interferon Regulatory Factor 3, a Subunit of Double-Stranded RNA-Activated Factor 1." Molecular and Cellular Biology 20, no. 11 (2000): 4159–68. http://dx.doi.org/10.1128/mcb.20.11.4159-4168.2000.

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ABSTRACT Viral double-stranded RNA (dsRNA) generated during the course of infection leads to the activation of a latent transcription factor, dsRNA-activated factor 1 (DRAF1). DRAF1 binds to a DNA target containing the type I interferon-stimulated response element and induces transcription of responsive genes. DRAF1 is a multimeric transcription factor containing the interferon regulatory factor 3 (IRF-3) protein and one of the histone acetyl transferases, CREB binding protein (CBP) or p300 (CBP/p300). In uninfected cells, the IRF-3 component of DRAF1 resides in the cytoplasm. The cytoplasmic

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10

De Jesús-González, Luis Adrián, Selvin Palacios-Rápalo, José Manuel Reyes-Ruiz, et al. "The Nuclear Pore Complex Is a Key Target of Viral Proteases to Promote Viral Replication." Viruses 13, no. 4 (2021): 706. http://dx.doi.org/10.3390/v13040706.

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Various viruses alter nuclear pore complex (NPC) integrity to access the nuclear content favoring their replication. Alteration of the nuclear pore complex has been observed not only in viruses that replicate in the nucleus but also in viruses with a cytoplasmic replicative cycle. In this last case, the alteration of the NPC can reduce the transport of transcription factors involved in the immune response or mRNA maturation, or inhibit the transport of mRNA from the nucleus to the cytoplasm, favoring the translation of viral mRNAs or allowing access to nuclear factors necessary for viral repli

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11

Jin, Chunyan, Randy Strich, and Katrina F. Cooper. "Slt2p phosphorylation induces cyclin C nuclear-to-cytoplasmic translocation in response to oxidative stress." Molecular Biology of the Cell 25, no. 8 (2014): 1396–407. http://dx.doi.org/10.1091/mbc.e13-09-0550.

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The yeast C-type cyclin represses the transcription of genes required for the stress response and meiosis. To relieve this repression, cyclin C undergoes nuclear-to-cytoplasmic translocation in response to many stressors, including hydrogen peroxide, where it is destroyed by ubiquitin-mediated proteolysis. Before its destruction, cyclin C promotes stress-induced mitochondrial fission and programmed cell death, indicating that relocalization is an important cell fate regulator. Here we show that cyclin C cytoplasmic translocation requires the cell wall integrity (CWI) mitogen-activated protein

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Jagla, Monika, Marie Fève, Pascal Kessler, et al. "A Splicing Variant of the Androgen Receptor Detected in a Metastatic Prostate Cancer Exhibits Exclusively Cytoplasmic Actions." Endocrinology 148, no. 9 (2007): 4334–43. http://dx.doi.org/10.1210/en.2007-0446.

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The androgen receptor (AR) is a ligand-activated transcription factor that displays genomic actions characterized by binding to androgen-response elements in the promoter of target genes as well as nongenomic actions that do not require nuclear translocation and DNA binding. In this study, we report exclusive cytoplasmic actions of a splicing variant of the AR detected in a metastatic prostate cancer. This AR variant, named AR23, results from an aberrant splicing of intron 2, wherein the last 69 nucleotides of the intronic sequence are retained, leading to the insertion of 23 amino acids betwe

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Leff, T. "AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins." Biochemical Society Transactions 31, no. 1 (2003): 224–27. http://dx.doi.org/10.1042/bst0310224.

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One of the primary functions of AMP-activated protein kinase (AMPK) is to regulate the metabolic pathways in response to reduced cellular energy charge. Most of the known targets of the kinase are cytoplasmic enzymes involved in both catabolic and anabolic metabolism. In addition, activation of AMPK in many cells results in changes in the pattern of gene expression. Although some of these effects are undoubtedly secondary responses to modified cellular metabolism, it is possible that in addition to its well-characterized function in the cytoplasm, AMPK also directly phosphorylates and regulate

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14

Bejarano, Pablo A., and Fathema Mousavi. "Incidence and Significance of Cytoplasmic Thyroid Transcription Factor-1 Immunoreactivity." Archives of Pathology & Laboratory Medicine 127, no. 2 (2003): 193–95. http://dx.doi.org/10.5858/2003-127-193-iasoct.

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Abstract Context.—The immunohistochemical identification of thyroid transcription factor-1 (TTF-1) is regarded as the presence of a nuclear pattern of staining and is used to identify tumors of thyroid or pulmonary origin. Although there have been reports of cytoplasmic expression of TTF-1, the significance of this pattern has not been studied in detail. Objectives.—To determine the incidence at which cytoplasmic immunostaining for TTF-1 occurs and to analyze the diagnostic value of this pattern of immunoreactivity. Design.—Histologic sections of 361 consecutive cases of neoplasms stained for

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Tijms, Marieke A., Yvonne van der Meer, and Eric J. Snijder. "Nuclear localization of non-structural protein 1 and nucleocapsid protein of equine arteritis virus." Journal of General Virology 83, no. 4 (2002): 795–800. http://dx.doi.org/10.1099/0022-1317-83-4-795.

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RNA synthesis (genome replication and subgenomic mRNA transcription) directed by equine arteritis virus (EAV; family Arteriviridae, order Nidovirales) occurs on modified cytoplasmic membranes to which most viral replicase subunits localize. Remarkably, a fraction of non-structural protein 1 (nsp1), a protein essential for transcription but dispensable for genome replication, is present in the host cell nucleus, in particular during the earlier stages of infection. Expression of GFP-tagged fusion proteins revealed that nsp1 is actively imported into the nucleus. Although the signals responsible

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Pan, Feng, Stefan Hüttelmaier, Robert H. Singer та Wei Gu. "ZBP2 Facilitates Binding of ZBP1 to β-Actin mRNA during Transcription". Molecular and Cellular Biology 27, № 23 (2007): 8340–51. http://dx.doi.org/10.1128/mcb.00972-07.

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ABSTRACT Cytoplasmic mRNA localization regulates gene expression by spatially restricting protein translation. Recent evidence has shown that nuclear proteins (such as hnRNPs) are required to form mRNPs capable of cytoplasmic localization. ZBP1 and ZBP2, two hnRNP K homology domain-containing proteins, were previously identified by their binding to the zipcode, the sequence element necessary and sufficient for β-actin mRNA localization. ZBP1 colocalizes with nascent β-actin mRNA in the nucleus but is predominantly a cytoplasmic protein. ZBP2, in contrast, is predominantly nuclear. We hypothesi

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Paroni, Gabriela, Michela Mizzau, Clare Henderson, Giannino Del Sal, Claudio Schneider, and Claudio Brancolini. "Caspase-dependent Regulation of Histone Deacetylase 4 Nuclear-Cytoplasmic Shuttling Promotes Apoptosis." Molecular Biology of the Cell 15, no. 6 (2004): 2804–18. http://dx.doi.org/10.1091/mbc.e03-08-0624.

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Histone deacetylases (HDACs) are important regulators of gene expression as part of transcriptional corepressor complexes. Here, we demonstrate that caspases can repress the activity of the myocyte enhancer factor (MEF)2C transcription factor by regulating HDAC4 processing. Cleavage of HDAC4 occurs at Asp 289 and disjoins the carboxy-terminal fragment, localized into the cytoplasm, from the amino-terminal fragment, which accumulates into the nucleus. In the nucleus, the caspase-generated fragment of HDAC4 is able to trigger cytochrome c release from mitochondria and cell death in a caspase-9–d

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Prescott, Jason D., Karen S. N. Koto, Meenakshi Singh, and Arthur Gutierrez-Hartmann. "The ETS Transcription Factor ESE-1 Transforms MCF-12A Human Mammary Epithelial Cells via a Novel Cytoplasmic Mechanism." Molecular and Cellular Biology 24, no. 12 (2004): 5548–64. http://dx.doi.org/10.1128/mcb.24.12.5548-5564.2004.

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ABSTRACT Several different transcription factors, including estrogen receptor, progesterone receptor, and ETS family members, have been implicated in human breast cancer, indicating that transcription factor-induced alterations in gene expression underlie mammary cell transformation. ESE-1 is an epithelium-specific ETS transcription factor that contains two distinguishing domains, a serine- and aspartic acid-rich (SAR) domain and an AT hook domain. ESE-1 is abundantly expressed in human breast cancer and trans-activates epithelium-specific gene promoters in transient transfection assays. While

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Chiribau, Calin-Bogdan, Francesca Gaccioli, Charlie C. Huang, Celvie L. Yuan та Maria Hatzoglou. "Molecular Symbiosis of CHOP and C/EBPβ Isoform LIP Contributes to Endoplasmic Reticulum Stress-Induced Apoptosis". Molecular and Cellular Biology 30, № 14 (2010): 3722–31. http://dx.doi.org/10.1128/mcb.01507-09.

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ABSTRACT Induction of the transcription factor CHOP (CCAAT-binding homologous protein; GADD 153) is a critical cellular response for the transcriptional control of endoplasmic reticulum (ER) stress-induced apoptosis. Upon nuclear translocation, CHOP upregulates the transcription of proapoptotic factors and downregulates antiapoptotic genes. Transcriptional activation by CHOP involves heterodimerization with other members of the basic leucine zipper transcription factor (bZIP) family. We show that the bZIP protein C/EBPβ isoform LIP is required for nuclear translocation of CHOP during ER stress

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Khacho, Mireille, Karim Mekhail, Karine Pilon-Larose, Josianne Payette, and Stephen Lee. "Cancer-Causing Mutations in a Novel Transcription-Dependent Nuclear Export Motif of VHL Abrogate Oxygen-Dependent Degradation of Hypoxia-Inducible Factor." Molecular and Cellular Biology 28, no. 1 (2007): 302–14. http://dx.doi.org/10.1128/mcb.01044-07.

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ABSTRACT It is thought that degradation of nuclear proteins by the ubiquitylation system requires nuclear-cytoplasmic trafficking of E3 ubiquitin ligases. The von Hippel-Lindau (VHL) tumor suppressor protein is the substrate recognition component of a Cullin-2-containing E3 ubiquitin ligase that recruits hypoxia-inducible factor (HIF) for oxygen-dependent degradation. We demonstrated that VHL engages in nuclear-cytoplasmic trafficking that requires ongoing transcription to promote efficient HIF degradation. Here, we report the identification of a discreet motif, DXGX2DX2L, that directs transcr

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Albertini, Markus, Lucy F. Pemberton, Jonathan S. Rosenblum, and Günter Blobel. "A Novel Nuclear Import Pathway for the Transcription Factor TFIIS." Journal of Cell Biology 143, no. 6 (1998): 1447–55. http://dx.doi.org/10.1083/jcb.143.6.1447.

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We have identified a novel pathway for protein import into the nucleus. We have shown that the previously identified but uncharacterized yeast protein Nmd5p functions as a karyopherin. It was therefore designated Kap119p (karyopherin with Mr of 119 kD). We localized Kap119p to both the nucleus and the cytoplasm. We identified the transcription elongation factor TFIIS as its major cognate import substrate. The cytoplasmic Kap119p exists as an approximately stoichiometric complex with TFIIS. RanGTP, not RanGDP, dissociated the isolated Kap119p/TFIIS complex and bound to Kap119p. Kap119p also bou

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Chaiseha, Y., Z. Tong, OM Youngren, and ME El Halawani. "Transcriptional changes in hypothalamic vasoactive intestinal peptide during a photo-induced reproductive cycle in the turkey." Journal of Molecular Endocrinology 21, no. 3 (1998): 267–75. http://dx.doi.org/10.1677/jme.0.0210267.

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To characterize further vasoactive intestinal peptide (VIP) as the prolactin-releasing factor in avian species, the present study examined hypothalamic VIP transcription and plasma prolactin (PRL) levels during the turkey reproductive cycle. The contribution of transcription to hypothalamic VIP mRNA steady-state levels and VIP content in response to gonadal stimulating photoperiod was also investigated. Nuclear run-on transcription assays were performed using nuclei isolated from hypothalami. Cytoplasmic VIP mRNA levels, and VIP content in the median eminence and plasma PRL levels were determi

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Romero, Nuria M., Maximiliano Irisarri, Peggy Roth, Ana Cauerhff, Christos Samakovlis та Pablo Wappner. "Regulation of the Drosophila Hypoxia-Inducible Factor α Sima by CRM1-Dependent Nuclear Export". Molecular and Cellular Biology 28, № 10 (2008): 3410–23. http://dx.doi.org/10.1128/mcb.01027-07.

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ABSTRACT Hypoxia-inducible factor α (HIF-α) proteins are regulated by oxygen levels through several different mechanisms that include protein stability, transcriptional coactivator recruitment, and subcellular localization. It was previously reported that these transcription factors are mainly nuclear in hypoxia and cytoplasmic in normoxia, but so far the molecular basis of this regulation is unclear. We show here that the Drosophila melanogaster HIF-α protein Sima shuttles continuously between the nucleus and the cytoplasm. We identified the relevant nuclear localization signal and two functi

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Groulx, Isabelle, and Stephen Lee. "Oxygen-Dependent Ubiquitination and Degradation of Hypoxia-Inducible Factor Requires Nuclear-Cytoplasmic Trafficking of the von Hippel-Lindau Tumor Suppressor Protein." Molecular and Cellular Biology 22, no. 15 (2002): 5319–36. http://dx.doi.org/10.1128/mcb.22.15.5319-5336.2002.

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ABSTRACT It is becoming increasingly evident that the degradation of nuclear proteins requires nuclear-cytoplasmic trafficking of both the substrate proteins, as well as the E3 ubiquitin-ligases. Here, we show that nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein (VHL) is required for oxygen-dependent ubiquitination and degradation of the alpha subunits of hypoxia-inducible factor (HIF-α). VHL engages in a constitutive transcription-sensitive nuclear-cytoplasmic shuttle unaffected by oxygen tension or levels of nuclear substrate HIF-α. Ubiquitinated forms of HI

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Mazanka, Emily, and Eric L. Weiss. "Sequential Counteracting Kinases Restrict an Asymmetric Gene Expression Program to early G1." Molecular Biology of the Cell 21, no. 16 (2010): 2809–20. http://dx.doi.org/10.1091/mbc.e10-02-0174.

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Gene expression is restricted to specific times in cell division and differentiation through close control of both activation and inactivation of transcription. In budding yeast, strict spatiotemporal regulation of the transcription factor Ace2 ensures that it acts only once in a cell's lifetime: at the M-to-G1 transition in newborn daughter cells. The Ndr/LATS family kinase Cbk1, functioning in a system similar to metazoan hippo signaling pathways, activates Ace2 and drives its accumulation in daughter cell nuclei, but the mechanism of this transcription factor's inactivation is unknown. We f

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Kulisz, Andre, and Hans-Georg Simon. "An Evolutionarily Conserved Nuclear Export Signal Facilitates Cytoplasmic Localization of the Tbx5 Transcription Factor." Molecular and Cellular Biology 28, no. 5 (2007): 1553–64. http://dx.doi.org/10.1128/mcb.00935-07.

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ABSTRACT During cardiac development, the T-box transcription factor Tbx5 displays dynamic changes in localization from strictly nuclear to both nuclear and cytoplasmic to exclusively cytoplasmic along the actin cytoskeleton in cells coexpressing its binding protein LMP4. Although nuclear localization signals (NLSs) have been described, the mechanism by which Tbx5 exits the nucleus remained elusive. Here, we describe for Tbx5 a nuclear export signal (NES) that is recognized by the CRM1 export protein. Site-directed mutagenesis of a critical amino acid(s) within this sequence determined the func

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Luo, Lingfei, Yvonne Uerlings, Nicole Happel, Naisana S. Asli, Hendrik Knoetgen, and Michael Kessel. "Regulation of Geminin Functions by Cell Cycle-Dependent Nuclear-Cytoplasmic Shuttling." Molecular and Cellular Biology 27, no. 13 (2007): 4737–44. http://dx.doi.org/10.1128/mcb.00123-07.

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ABSTRACT The geminin protein functions both as a DNA rereplication inhibitor through association with Cdt1 and as a repressor of Hox gene transcription through the polycomb pathway. Here, we report that the functions of avian geminin are coordinated with and regulated by cell cycle-dependent nuclear-cytoplasmic shuttling. In S phase, geminin enters nuclei and inhibits both loading of the minichromosome maintenance (MCM) complex onto chromatin and Hox gene transcription. At the end of mitosis, geminin is exported from nuclei by the exportin protein Crm1 and is unavailable in the nucleus during

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Khacho, Mireille, Karim Mekhail, Karine Pilon-Larose, Arnim Pause, Jocelyn Côté, and Stephen Lee. "eEF1A Is a Novel Component of the Mammalian Nuclear Protein Export Machinery." Molecular Biology of the Cell 19, no. 12 (2008): 5296–308. http://dx.doi.org/10.1091/mbc.e08-06-0562.

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The cytoplasmic translation factor eEF1A has been implicated in the nuclear export of tRNA species in lower eukaryotes. Here we demonstrate that eEF1A plays a central role in nuclear export of proteins in mammalian cells. TD-NEM (transcription-dependent nuclear export motif), a newly characterized nuclear export signal, mediates efficient nuclear export of several proteins including the von Hippel-Lindau (VHL) tumor suppressor and the poly(A)-binding protein (PABP1) in a manner that is dependent on ongoing RNA polymerase II (RNA PolII)-dependent transcription. eEF1A interacts specifically with

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Ducret, Catherine, Sauveur-Michel Maira, Andrée Dierich, and Bohdan Wasylyk. "The Net Repressor Is Regulated by Nuclear Export in Response to Anisomycin, UV, and Heat Shock." Molecular and Cellular Biology 19, no. 10 (1999): 7076–87. http://dx.doi.org/10.1128/mcb.19.10.7076.

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ABSTRACT The ternary complex factors (TCFs) are targets for Ras/mitogen-activated protein kinase signalling pathways. They integrate the transcriptional response at the level of serum response elements in early-response genes, such as the c-fosproto-oncogene. An important aim is to understand the individual roles played by the three TCFs, Net, Elk1, and Sap1a. Net, in contrast to Elk1 and Sap1a, is a strong repressor of transcription. We now show that Net is regulated by nuclear-cytoplasmic shuttling in response to specific signalling pathways. Net is mainly nuclear under both normal and basal

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Camarata, Troy, Benjamin Bimber, Andre Kulisz, Teng-Leong Chew, Jennifer Yeung, and Hans-Georg Simon. "LMP4 regulates Tbx5 protein subcellular localization and activity." Journal of Cell Biology 174, no. 3 (2006): 339–48. http://dx.doi.org/10.1083/jcb.200511109.

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The limb- and heart-specific Tbx5 transcription factor coexpresses with and directly binds to the novel PDZ-LIM domain protein, LMP4. LMP4 is distributed in the cytoplasm associated with the actin cytoskeleton. In the presence of LMP4, Tbx5 shuttles dynamically between the nucleus and cytoplasm and, in a complex with LMP4, localizes to actin filaments. Nuclear and cytoplasmic Tbx5 distribution in developing chicken wings suggests the functional significance of the LMP4–Tbx5 interaction. In primary epicardial cells, we demonstrate that Tbx5 protein subcellular relocalization can be stimulated b

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Raney, Anneke K., Carrie M. Eggers, Eric F. Kline та ін. "Nuclear Covalently Closed Circular Viral Genomic DNA in the Liver of Hepatocyte Nuclear Factor 1α-Null Hepatitis B Virus Transgenic Mice". Journal of Virology 75, № 6 (2001): 2900–2911. http://dx.doi.org/10.1128/jvi.75.6.2900-2911.2001.

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ABSTRACT The role of hepatocyte nuclear factor 1α (HNF1α) in the regulation of hepatitis B virus (HBV) transcription and replication in vivo was investigated using a HNF1α-null HBV transgenic mouse model. HBV transcription was not measurably affected by the absence of the HNF1α transcription factor. However, intracellular viral replication intermediates were increased two- to fourfold in mice lacking functional HNF1α protein. The increase in encapsidated cytoplasmic replication intermediates in HNF1α-null HBV transgenic mice was associated with the appearance of nonencapsidated nuclear covalen

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Xu, L., M. D. Joo, A. Mesalam, S. H. Song, S. Zhang, and I. K. Kong. "38 Improved Cloning Efficiency and Developmental Potential in Bovine Somatic Cell Nuclear Transfer with the New Technology." Reproduction, Fertility and Development 30, no. 1 (2018): 158. http://dx.doi.org/10.1071/rdv30n1ab38.

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Bovine somatic cell nuclear transfer (SCNT) embryos can develop to the blastocyst stage at a rate similar to that of embryos produced by IVF; however, its efficiency remains low. In this study, we examined the effects of cytoplasm restoration of enucleated oocyte, by injecting ~30% of the cytoplasm of a donor oocyte to restore the enucleated oocyte cytoplasm volume to normal, on the developmental competence and quality of bovine cloned embryos during pre-implantation using the TUNEL assay, quantitative reverse transcription PCR (RT-qPCR) and immunocytochemistry. The experiment was conducted in

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Tong, Z., GR Pitts, S. You, DN Foster, and ME El Halawani. "Vasoactive intestinal peptide stimulates turkey prolactin gene expression by increasing transcription rate and enhancing mRNA stability." Journal of Molecular Endocrinology 21, no. 3 (1998): 259–66. http://dx.doi.org/10.1677/jme.0.0210259.

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This study evaluates the transcriptional and post-transcriptional regulation of prolactin (PRL) by vasoactive intestinal peptide (VIP). Pituitary nuclei from laying (control), incubating (with enhanced VIP secretion), and VIP-immunized laying turkey hens, and from pituitary cells cultured with or without VIP were used in nuclear run-on transcription assays. Cytoplasmic PRL mRNA was analyzed by slot blot hybridization. PRL transcription was greater in hyperprolactinemic incubating birds (PRL/beta-actin=3.33) than in laying birds (PRL/beta-actin=1.83). VIP-immunoneutralized birds had 47% and 51%

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Staus, Dean P., Laura Weise-Cross, Kevin D. Mangum, et al. "Nuclear RhoA signaling regulates MRTF-dependent SMC-specific transcription." American Journal of Physiology-Heart and Circulatory Physiology 307, no. 3 (2014): H379—H390. http://dx.doi.org/10.1152/ajpheart.01002.2013.

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We have previously shown that RhoA-mediated actin polymerization stimulates smooth muscle cell (SMC)-specific transcription by regulating the nuclear localization of the myocardin-related transcription factors (MRTFs). On the basis of the recent demonstration that nuclear G-actin regulates MRTF nuclear export and observations from our laboratory and others that the RhoA effector, mDia2, shuttles between the nucleus and cytoplasm, we investigated whether nuclear RhoA signaling plays a role in regulating MRTF activity. We identified sequences that control mDia2 nuclear-cytoplasmic shuttling and

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Hazan, Renin, Munemasa Mori, Paul S. Danielian, et al. "E2F4’s cytoplasmic role in multiciliogenesis is mediated via an N-terminal domain that binds two components of the centriole replication machinery, Deup1 and SAS6." Molecular Biology of the Cell 32, no. 20 (2021): ar1. http://dx.doi.org/10.1091/mbc.e21-01-0039.

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Multiciliogenesis requires both nuclear and cytoplasmic functions of the E2F4 transcription factor. Here we identify a domain in E2F4 that interacts with two key components of the cytoplasmic centriole replication machinery, Deup1 and SAS6, and is sufficient to mediate E2F4’s cytoplasmic role in multiciliogenesis.

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Khurana, Simran, Sharmistha Chakraborty, Minh Lam та ін. "Familial Focal Segmental Glomerulosclerosis (FSGS)-linked α-Actinin 4 (ACTN4) Protein Mutants Lose Ability to Activate Transcription by Nuclear Hormone Receptors". Journal of Biological Chemistry 287, № 15 (2012): 12027–35. http://dx.doi.org/10.1074/jbc.m112.345421.

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Mutations in α-actinin 4 (ACTN4) are linked to familial forms of focal segmental glomerulosclerosis (FSGS), a kidney disease characterized by proteinuria due to podocyte injury. The mechanisms underlying ACTN4 mutant-associated FSGS are not completely understood. Although α-actinins are better known to cross-link actin filaments and modulate cytoskeletal organization, we have previously shown that ACTN4 interacts with transcription factors including estrogen receptor and MEF2s and potentiates their transcriptional activity. Nuclear receptors including retinoic acid receptor (RAR) have been pro

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Omnus, Deike J., and Per O. Ljungdahl. "Latency of transcription factor Stp1 depends on a modular regulatory motif that functions as cytoplasmic retention determinant and nuclear degron." Molecular Biology of the Cell 25, no. 23 (2014): 3823–33. http://dx.doi.org/10.1091/mbc.e14-06-1140.

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The Ssy1-Ptr3-Ssy5 (SPS)–sensing pathway enables yeast to respond to extracellular amino acids. Stp1, the effector transcription factor, is synthesized as a latent cytoplasmic precursor with an N-terminal regulatory domain that restricts its nuclear accumulation. The negative regulatory mechanisms impinging on the N-terminal domain are poorly understood. However, Stp1 latency depends on three inner nuclear membrane proteins, Asi1, Asi2, and Asi3. We report that the N-terminal domain of Stp1 contains a small motif, designated RI, that fully accounts for latency. RI is modular, mediates interact

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Kretz-Remy, Carole, Sébastien Michaud, and Robert M. Tanguay. "The nuclear chronicles: gene transcription and molecular traveling." Biochemistry and Cell Biology 77, no. 4 (1999): 243–47. http://dx.doi.org/10.1139/o99-045.

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The transfer and processing of an RNA transcript from its locus of transcription on chromatin through the nuclear membrane to its site of translation on cytoplasmic ribosomes is a long and complex journey involving numerous processes and interactions with various macromolecules. These various steps that regulate gene expression were the subject of the 9th Winternational Symposium of the Canadian Society of Biochemistry and Molecular & Cell Biology held at Manoir du Lac Delage, a small resort centre north of Québec City on February 12-15, 1999.Key words: nuclear pore, RNA transport, chromat

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Millán-Zambrano, Gonzalo, and Sebastián Chávez. "Nuclear functions of prefoldin." Open Biology 4, no. 7 (2014): 140085. http://dx.doi.org/10.1098/rsob.140085.

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Prefoldin is a cochaperone, present in all eukaryotes, that cooperates with the chaperonin CCT. It is known mainly for its functional relevance in the cytoplasmic folding of actin and tubulin monomers during cytoskeleton assembly. However, both canonical and prefoldin-like subunits of this heterohexameric complex have also been found in the nucleus, and are functionally connected with nuclear processes in yeast and metazoa. Plant prefoldin has also been detected in the nucleus and physically associated with a gene regulator. In this review, we summarize the information available on the involve

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Burton, Molly, Cherrag D. Upadhyaya, Bernhard Maier, Thomas J. Hope, and O. John Semmes. "Human T-Cell Leukemia Virus Type 1 Tax Shuttles between Functionally Discrete Subcellular Targets." Journal of Virology 74, no. 5 (2000): 2351–64. http://dx.doi.org/10.1128/jvi.74.5.2351-2364.2000.

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ABSTRACT Human T-cell leukemia virus type 1 (HTLV-1) Tax is a nuclear protein with striking pleiotropic functionality. We recently demonstrated that Tax localizes to a multicomponent nuclear speckled structure (Tax speckled structure [TSS]). Here, we examine these structures further and identify a partial overlap of TSS with transcription hot spots. We used a strategy of directed expression via fusion proteins to determine if these transcription sites are the subtargets within TSS required for Tax function. When fused to human immunodeficiency virus type 1 (HIV-1) Tat, the resulting Tat-Tax fu

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Cong, Feng, Liang Schweizer, Mario Chamorro та Harold Varmus. "Requirement for a Nuclear Function of β-Catenin in Wnt Signaling". Molecular and Cellular Biology 23, № 23 (2003): 8462–70. http://dx.doi.org/10.1128/mcb.23.23.8462-8470.2003.

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ABSTRACT Wnt signaling stabilizes β-catenin, which in turn influences the transcription of Wnt-responsive genes in conjunction with T-cell factor (TCF) transcription factors. At present, there are two models for the actions of β-catenin. The conventional nuclear model suggests that β-catenin acts in the nucleus to form a heterodimeric transcriptional factor complex with TCF, with TCF providing DNA-specific binding and the C and N termini of β-catenin stimulating transcription. The alternative cytoplasmic model postulates that β-catenin exports TCF from the nucleus to relieve its repressive act

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Sekito, Takayuki, Janet Thornton, and Ronald A. Butow. "Mitochondria-to-Nuclear Signaling Is Regulated by the Subcellular Localization of the Transcription Factors Rtg1p and Rtg3p." Molecular Biology of the Cell 11, no. 6 (2000): 2103–15. http://dx.doi.org/10.1091/mbc.11.6.2103.

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Cells modulate the expression of nuclear genes in response to changes in the functional state of mitochondria, an interorganelle communication pathway called retrograde regulation. In yeast, expression of the CIT2 gene shows a typical retrograde response in that its expression is dramatically increased in cells with dysfunctional mitochondria, such as in ρo petites. Three genes control this signaling pathway: RTG1 andRTG3, which encode basic helix-loop-helix leucine zipper transcription factors that bind as heterodimer to theCIT2 upstream activation site, and RTG2, which encodes a protein of u

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Chestukhin, Anton, Larisa Litovchick, Katherine Rudich, and James A. DeCaprio. "Nucleocytoplasmic Shuttling of p130/RBL2: Novel Regulatory Mechanism." Molecular and Cellular Biology 22, no. 2 (2002): 453–68. http://dx.doi.org/10.1128/mcb.22.2.453-468.2002.

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ABSTRACT The retinoblastoma-related pocket proteins pRb, p107, and p130 are implicated in the control of cell proliferation, differentiation, and transformation. The function of pocket proteins is in part mediated by their ability to inhibit specific E2F transcription factors. The transcriptional activity of E2Fs is controlled by alteration of their nucleocytoplasmic localization during the cell cycle. p130 was observed to shuttle between the nucleus and cytoplasm in a heterokaryon fusion assay, suggesting the presence of nuclear and cytoplasmic localization signals. Two independent nuclear lo

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Oguchi, Yusuke, Yuka Ozaki, Mahmoud N. Abdelmoez, and Hirofumi Shintaku. "NanoSINC-seq dissects the isoform diversity in subcellular compartments of single cells." Science Advances 7, no. 15 (2021): eabe0317. http://dx.doi.org/10.1126/sciadv.abe0317.

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Alternative mRNA isoforms play a key role in generating diverse protein isoforms. To dissect isoform usage in the subcellular compartments of single cells, we introduced an novel approach, nanopore sequencing coupled with single-cell integrated nuclear and cytoplasmic RNA sequencing, that couples microfluidic fractionation, which separates cytoplasmic RNA from nuclear RNA, with full-length complementary DNA (cDNA) sequencing using a nanopore sequencer. Leveraging full-length cDNA reads, we found that the nuclear transcripts are notably more diverse than cytoplasmic transcripts. Our findings al

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Beaudoin, Jude, and Simon Labbé. "Copper Induces Cytoplasmic Retention of Fission Yeast Transcription Factor Cuf1." Eukaryotic Cell 5, no. 2 (2006): 277–92. http://dx.doi.org/10.1128/ec.5.2.277-292.2006.

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ABSTRACT Copper homeostasis within the cell is established and preserved by different mechanisms. Changes in gene expression constitute a way of maintaining this homeostasis. In Schizosaccharomyces pombe, the Cuf1 transcription factor is critical for the activation of copper transport gene expression under conditions of copper starvation. However, in the presence of elevated intracellular levels of copper, the mechanism of Cuf1 inactivation to turn off gene expression remains unclear. In this study, we provide evidence that inactivation of copper transport gene expression by Cuf1 is achieved t

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Alvandi, Zahra, and Michal Opas. "c-Src kinase inhibits osteogenic differentiation via enhancing STAT1 stability." PLOS ONE 15, no. 11 (2020): e0241646. http://dx.doi.org/10.1371/journal.pone.0241646.

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The proto-oncogene Src is ubiquitously expressed and is involved in cellular differentiation. However, the role of Src in embryonic stem (ES) cell osteogenic differentiation is largely unknown. Using the small molecule inhibitor PP2, c-Src specific siRNAs, and tet-inducible lentiviral vectors overexpressing active c-Src, we delineated an inhibitory role of c-Src in osteogenic differentiation of mouse embryonic stem cells (mESCs) and mouse MC3T3-E1s preosteoblasts. Active c-Src was shown to restrict the nuclear residency of Runt-related transcription factor 2 (Runx2) and its transcriptional act

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Li, Feng-Qian, Adaobi Mofunanya, Victoria Fischer, Jason Hall та Ken-Ichi Takemaru. "Nuclear-Cytoplasmic Shuttling of Chibby Controls β-Catenin Signaling". Molecular Biology of the Cell 21, № 2 (2010): 311–22. http://dx.doi.org/10.1091/mbc.e09-05-0437.

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In the canonical Wnt pathway, β-catenin acts as a key coactivator that stimulates target gene expression through interaction with Tcf/Lef transcription factors. Its nuclear accumulation is the hallmark of active Wnt signaling and is frequently associated with cancers. Chibby (Cby) is an evolutionarily conserved molecule that represses β-catenin–dependent gene activation. Although Cby, in conjunction with 14-3-3 chaperones, controls β-catenin distribution, its molecular nature remains largely unclear. Here, we provide compelling evidence that Cby harbors bona fide nuclear localization signal (N

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Syed, Sahla, Henry Wilky, João Raimundo, Bomyi Lim, and Amanda A. Amodeo. "The nuclear to cytoplasmic ratio directly regulates zygotic transcription inDrosophilathrough multiple modalities." Proceedings of the National Academy of Sciences 118, no. 14 (2021): e2010210118. http://dx.doi.org/10.1073/pnas.2010210118.

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Early embryos must rapidly generate large numbers of cells to form an organism. Many species accomplish this through a series of rapid, reductive, and transcriptionally silent cleavage divisions. Previous work has demonstrated that the number of divisions before both cell cycle elongation and zygotic genome activation (ZGA) is regulated by the ratio of nuclear content to cytoplasm (N/C). To understand how the N/C ratio affects the timing of ZGA, we directly assayed the behavior of several previously identified N/C ratio–dependent genes using the MS2-MCP reporter system in livingDrosophilaembry

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Dehghani, Hesam, Cara Reith та Ann C. Hahnel. "Subcellular localization of protein kinase C δ and ε affects transcriptional and post-transcriptional processes in four-cell mouse embryos". Reproduction 130, № 4 (2005): 453–65. http://dx.doi.org/10.1530/rep.1.00572.

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During mouse preimplantation development, two isozymes of protein kinase C (PKC), δ and ε, transiently localize to nuclei at the early four-cell stage. In order to study their functions at this stage, we altered the subcellular localization of these isozymes (ratio of nuclear to cytoplasmic concentrations) with peptides that specifically activate or inhibit translocation of each isozyme. The effects of altering nuclear concentration of each isozyme on transcription (5-bromouridine 5′-triphosphate (BrUTP) incorporation), amount and distribution of small nuclear ribonucleoproteins (snRNPs), nucl

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Estruch, Francisco, and Charles N. Cole. "An Early Function during Transcription for the Yeast mRNA Export Factor Dbp5p/Rat8p Suggested by Its Genetic and Physical Interactions with Transcription Factor IIH Components." Molecular Biology of the Cell 14, no. 4 (2003): 1664–76. http://dx.doi.org/10.1091/mbc.e02-09-0602.

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The yeast DEAD-box protein Dbp5p/Rat8p is an essential factor for mRNA export and shuttles between the nucleus and the cytoplasm. It is concentrated at the cytoplasmic fibrils of the nuclear pore complex where it interacts with several nucleoporins. On the basis of this localization, it has been suggested that it might participate in a terminal step of RNA export, the release from the mRNA of proteins that accompany the mRNA during translocation through nuclear pores. In this report, we present evidence linking Dbp5p to transcription. Two different screens identified genetic interactions betwe

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