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1

Murray, M. T., G. Krohne, and W. W. Franke. "Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos." Journal of Cell Biology 112, no. 1 (1991): 1–11. http://dx.doi.org/10.1083/jcb.112.1.1.

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To gain insight into the mechanisms involved in the formation of maternally stored mRNPs during Xenopus laevis development, we searched for soluble cytoplasmic proteins of the oocyte that are able to selectively bind mRNAs, using as substrate radiolabeled mRNA. In vitro mRNP assembly in solution was followed by UV-cross-linking and RNase digestion, resulting in covalent tagging of polypeptides by nucleotide transfer. Five polypeptides of approximately 54, 56 60, 70, and 100 kD (p54, p56, p60, p70, and p100) have been found to selectively bind mRNA and assemble into mRNPs. These polypeptides, w
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2

Legagneux, V., P. Bouvet, F. Omilli, S. Chevalier, and H. B. Osborne. "Identification of RNA-binding proteins specific to Xenopus Eg maternal mRNAs: association with the portion of Eg2 mRNA that promotes deadenylation in embryos." Development 116, no. 4 (1992): 1193–202. http://dx.doi.org/10.1242/dev.116.4.1193.

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Maternal Xenopus Eg mRNAs have been previously identified as transcripts that are specifically deadenylated after fertilization and degraded after the mid blastula transition. Destabilizing cis sequences were previously localised in the 3′ untranslated region of Eg2 mRNA. In order to characterize possible trans-acting factors which are involved in the post-transcriptional regulation of Eg mRNAs, gel-shift and u.v. cross-linking experiments were performed, which allowed the identification of a p53-p55 RNA-binding protein doublet specific for the 3′ untranslated regions of Eg mRNAs. These p53-p5
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3

Minshall, Nicola, Michel Kress, Dominique Weil, and Nancy Standart. "Role of p54 RNA Helicase Activity and Its C-terminal Domain in Translational Repression, P-body Localization and Assembly." Molecular Biology of the Cell 20, no. 9 (2009): 2464–72. http://dx.doi.org/10.1091/mbc.e09-01-0035.

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The RNA helicase p54 (DDX6, Dhh1, Me31B, Cgh-1, RCK) is a prototypic component of P-(rocessing) bodies in cells ranging from yeast to human. Previously, we have shown that it is also a component of the large cytoplasmic polyadenylation element-binding protein translation repressor complex in Xenopus oocytes and that when tethered to the 3′ untranslated region, Xp54 represses reporter mRNA translation. Here, we examine the role of the p54 helicase activity in translational repression and in P-body formation. Mutagenesis of conserved p54 helicase motifs activates translation in the tethered func
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4

Ohsumi, T., T. Ichimura, H. Sugano, S. Omata, T. Isobe, and R. Kuwano. "Ribosome-binding protein p34 is a member of the leucine-rich-repeat-protein superfamily." Biochemical Journal 294, no. 2 (1993): 465–72. http://dx.doi.org/10.1042/bj2940465.

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Protein p34 is a non-glycosylated membrane protein characteristic of rough microsomes and is believed to play a role in the ribosome-membrane association. In the present study we isolated cDNA encoding p34 from a rat liver cDNA library and determined its complete amino acid sequence. p34 mRNA is 3.2 kb long and encodes a polypeptide of 307 amino acids with a molecular mass of about 34.9 kDa. Primary sequence analysis, coupled with biochemical studies on the topology, suggested that p34 is a type II signal-anchor protein; it is composed of a large cytoplasmic domain, a membrane-spanning segment
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5

Yang, M., Z. Fan, and I. A. Polejaeva. "1 Microinjection of CPE-Binding Protein Polyadenylated mRNA Increases Developmental Competence of Bovine Oocytes In Vitro." Reproduction, Fertility and Development 30, no. 1 (2018): 140. http://dx.doi.org/10.1071/rdv30n1ab1.

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Developmental competence is acquired during oocyte growth and maturation while oocytes undergo both nuclear and cytoplasmic changes. Completion of oocyte maturation and subsequent embryo development relies mostly on maternally synthesised and stored mRNAs at the transcriptionally quiescent phase. The temporal and spatial post-transcriptional and translational regulation of the stored mRNA in mammalian oocyte cytoplasm is essential for developmental competence of oocytes and is often controlled via cytoplasmic polyadenylation. Cytoplasmic polyadenylation element (CPE)-binding protein (CPEB) is
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6

Galbán, Stefanie, Jennifer L. Martindale, Krystyna Mazan-Mamczarz, et al. "Influence of the RNA-Binding Protein HuR in pVHL-Regulated p53 Expression in Renal Carcinoma Cells." Molecular and Cellular Biology 23, no. 20 (2003): 7083–95. http://dx.doi.org/10.1128/mcb.23.20.7083-7095.2003.

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ABSTRACT A recent analysis of gene expression in renal cell carcinoma cells led to the identification of mRNAs whose translation was dependent on the presence of the von Hippel-Lindau (VHL) tumor suppressor gene product, pVHL. Here, we investigate the finding that pVHL-expressing RCC cells (VHL+) exhibited elevated levels of polysome-associated p53 mRNA and increased p53 protein levels compared with VHL-defective (VHL−) cells. Our findings indicate that p53 translation is specifically heightened in VHL+ cells, given that (i) p53 mRNA abundance in VHL+ and VHL− cells was comparable, (ii) p53 de
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7

Xiao, Lan, Jaladanki N. Rao, Tongtong Zou, et al. "Polyamines Regulate the Stability of Activating Transcription Factor-2 mRNA through RNA-binding Protein HuR in Intestinal Epithelial Cells." Molecular Biology of the Cell 18, no. 11 (2007): 4579–90. http://dx.doi.org/10.1091/mbc.e07-07-0675.

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Maintenance of intestinal mucosal epithelial integrity requires polyamines that modulate the expression of various genes involved in cell proliferation and apoptosis. Recently, polyamines were shown to regulate the subcellular localization of the RNA-binding protein HuR, which stabilizes its target transcripts such as nucleophosmin and p53 mRNAs. The activating transcription factor-2 (ATF-2) mRNA encodes a member of the ATF/CRE-binding protein family of transcription factors and was computationally predicted to be a target of HuR. Here, we show that polyamines negatively regulate ATF-2 express
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8

Lafarga, Vanesa, Ana Cuadrado, Isabel Lopez de Silanes, Rocio Bengoechea, Oscar Fernandez-Capetillo, and Angel R. Nebreda. "p38 Mitogen-Activated Protein Kinase- and HuR-Dependent Stabilization of p21Cip1 mRNA Mediates the G1/S Checkpoint." Molecular and Cellular Biology 29, no. 16 (2009): 4341–51. http://dx.doi.org/10.1128/mcb.00210-09.

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ABSTRACT Activation of p38 mitogen-activated protein kinase (MAPK) plays an important role in the G2/M cell cycle arrest induced by DNA damage, but little is known about the role of this signaling pathway in the G1/S transition. Upregulation of the cyclin-dependent kinase inhibitor p21Cip1 is thought to make a major contribution to the G1/S cell cycle arrest induced by γ radiation. We show here that inhibition of p38 MAPK impairs p21Cip1 accumulation and, as a result, the ability of cells to arrest in G1 in response to γ radiation. We found that p38 MAPK induces p21Cip1 mRNA stabilization, wit
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9

Gabler, Stefan, Holger Schütt, Peter Groitl, Hans Wolf, Thomas Shenk, and Thomas Dobner. "E1B 55-Kilodalton-Associated Protein: a Cellular Protein with RNA-Binding Activity Implicated in Nucleocytoplasmic Transport of Adenovirus and Cellular mRNAs." Journal of Virology 72, no. 10 (1998): 7960–71. http://dx.doi.org/10.1128/jvi.72.10.7960-7971.1998.

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ABSTRACT The adenovirus type 5 (Ad5) early 1B 55-kDa protein (E1B-55kDa) is a multifunctional phosphoprotein that regulates viral DNA replication and nucleocytoplasmic RNA transport in lytically infected cells. In addition, E1B-55kDa provides functions required for complete oncogenic transformation of rodent cells in cooperation with the E1A proteins. Using the far-Western technique, we have isolated human genes encoding E1B-55kDa-associated proteins (E1B-APs). The E1B-AP5 gene encodes a novel nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family that is hig
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10

Ramalingam, Satish, Gopalan Natarajan, Chris Schafer, et al. "Novel intestinal splice variants of RNA-binding protein CUGBP2: isoform-specific effects on mitotic catastrophe." American Journal of Physiology-Gastrointestinal and Liver Physiology 294, no. 4 (2008): G971—G981. http://dx.doi.org/10.1152/ajpgi.00540.2007.

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CUG triplet repeat-binding protein 2 (CUGBP2) is a RNA-binding protein that regulates mRNA translation and modulates apoptosis. Here, we report the identification of two splice variants (termed variants 2 and 3) in cultured human intestinal epithelial cells and in mouse gastrointestinal tract. The variants are generated from alternative upstream promoters resulting in the inclusion of additional NH2-terminal residues. Although variant 2 is the predominant isoform in normal intestine, its expression is reduced, whereas variant 1 is overexpressed following γ-irradiation. All three variants bind
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11

INOUE, Akira, Yukitomo ARAO, Akira OMORI, et al. "Identification of S1 proteins B2, C1 and D1 as AUF1 isoforms and their major role as heterogeneous nuclear ribonucleoprotein proteins." Biochemical Journal 372, no. 3 (2003): 775–85. http://dx.doi.org/10.1042/bj20021719.

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AUF1 (A+U-rich RNA binding factor) participates in the rapid decay of mRNAs in the cytoplasm. It is sometimes called heterogeneous nuclear ribonucleoprotein (hnRNP) D0; however, evidence for its characterization as an hnRNP protein has been scarce. S1 proteins A–D are those selectively extracted at pH 4.9 from isolated nuclei pretreated with either RNase A or DNase I. In the present study we identified S1 (‘first supernatant’) proteins B2, C1 and D1 with p45, p40 and p37 AUF1s respectively, by microsequencing and product analysis of transfected cDNAs. We found, further, that more than 96% of t
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12

Lu, Zhi Hong, Jason T. Books, and Timothy James Ley. "The Cold-Shock Domain Protein YB-1 Is Important for Cellular Proliferation and the Prevention of Premature Senescence." Blood 104, no. 11 (2004): 2571. http://dx.doi.org/10.1182/blood.v104.11.2571.2571.

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Abstract Mammalian proteins containing “cold-shock” domains belong to the most evolutionarily conserved family of nucleic acid-binding proteins known in bacteria, plants, and animals. One of these proteins, YB-1, has been implicated in basic cellular functions such as cell proliferation and responses to environmental stresses. In mammalian cells, YB-1 has been shown to shuttle between the nuclear and cytoplasmic compartments. Within the nucleus, YB-1 interacts with several DNA-and pre-mRNA-binding proteins, and has been implicated in nuclear activities, including transcriptional regulation, ch
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13

Kung, Che-Pei, and Nancy Raab-Traub. "Epstein-Barr Virus Latent Membrane Protein 1 Induces Expression of the Epidermal Growth Factor Receptor through Effects on Bcl-3 and STAT3." Journal of Virology 82, no. 11 (2008): 5486–93. http://dx.doi.org/10.1128/jvi.00125-08.

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ABSTRACT Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) activates multiple signaling pathways. Two regions, C-terminal-activating region 1 (CTAR1) and CTAR2, have been identified within the cytoplasmic carboxy terminal domain that activates NF-κB. CTAR2 activates the canonical NF-κB pathway, which includes p50/p65 complexes. CTAR1 can activate both the canonical and noncanonical pathways to produce multiple distinct NF-κB dimers, including p52/p50, p52/p65, and p50/p50. CTAR1 also uniquely upregulates the epidermal growth factor receptor (EGFR) in epithelial cells. Increased p50-Bcl
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14

Lewis, Michael I., Sue C. Bodine, Nader Kamangar, Xuan Xu, Xiaoyu Da, and Mario Fournier. "Effect of severe short-term malnutrition on diaphragm muscle signal transduction pathways influencing protein turnover." Journal of Applied Physiology 100, no. 6 (2006): 1799–806. http://dx.doi.org/10.1152/japplphysiol.01233.2005.

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The aim of this study was to evaluate the effect of nutritional deprivation (ND) on signal transduction pathways influencing the translational apparatus in the diaphragm muscle. Male rats were divided into two groups: 1) 20% of usual food intake for 4 days (ND) with water provided at libitum and 2) free-eating control (Ctl). Total protein and RNA were extracted from the diaphragm. Insulin-like growth factor I mRNA was analyzed by RT-PCR. Protein analyses of key cytoplasmic proteins for three signaling pathways deemed important in influencing protein turnover [phosphatidylinositol 3-kinase- Akt
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15

Tagoug, Ines, Paola Neri, Jiri Slaby, et al. "XPO1 Inhibition Disrupts Ribosomal Subunits Assembly and Induces Multiple Myeloma (MM) Cell Death." Blood 122, no. 21 (2013): 3165. http://dx.doi.org/10.1182/blood.v122.21.3165.3165.

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Abstract Background Chromosomal region maintenance (CRM1), also known as exportin 1 (XPO1) plays an important role in the nuclear-cytoplasmic shuttling. The nuclear export receptor, XPO1, is considered as a regulator of subcellular distribution of several proteins involved in the regulation of centrosome duplication such as nucleophosmin (NPM), breast and ovarian cancer susceptibility protein 1 (BRCA1) and many tumor suppressor proteins (p53, p21, FOXO and pRB). Furthermore, XPO1 is required for the export of assembled ribosomal subunits (60S & 40S) from the nucleolus back into the cytopla
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16

Timar, Botond, Amy Chadburn, Daniel Knowles, and Ethel Cesarman. "Activation of Classical and Alternative Nuclear Factor-kappaB (NF-kB) Pathways in Diffuse Large B-Cell Lymphomas." Blood 104, no. 11 (2004): 29. http://dx.doi.org/10.1182/blood.v104.11.29.29.

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Abstract Activation of the NF-kB pathway is involved in many human neoplasms. In this study we examined the status of the NF-kB canonical (IkB, p50/p65) and non-canonical (p52, RelB) pathways in diffuse large B-cell lymphomas (DLBCL), which are a common and heterogeneous group of lymphoid malignancies. DLBCL have been divided into activated B-cell (ABC) like, and germinal center B-cell (GCB) like subgroups, which have been reported to have high and low NF-kB activity, respectively. However, the nature of the NF-kB complexes in this lymphoma entity has not been previously evaluated. Therefore w
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17

Mittal, Saloni, Akhmed Aslam, Rachel Doidge, Rachel Medica, and G. Sebastiaan Winkler. "The Ccr4a (CNOT6) and Ccr4b (CNOT6L) deadenylase subunits of the human Ccr4–Not complex contribute to the prevention of cell death and senescence." Molecular Biology of the Cell 22, no. 6 (2011): 748–58. http://dx.doi.org/10.1091/mbc.e10-11-0898.

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A key step in cytoplasmic mRNA degradation is the shortening of the poly(A) tail, which involves several deadenylase enzymes. Relatively little is known about the importance of these enzymes for the cellular physiology. Here we focused on the role of the highly similar Ccr4a (CNOT6) and Ccr4b (CNOT6L) deadenylase subunits of the Ccr4–Not complex. In addition to a role in cell proliferation, Ccr4a and Ccr4b play a role in cell survival, in contrast to the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits or the CNOT1 and CNOT3 noncatalytic subunits of the Ccr4–Not complex. Underscoring the d
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18

McDonald, Patrick P., Anette Bald та Marco A. Cassatella. "Activation of the NF-κB Pathway by Inflammatory Stimuli in Human Neutrophils". Blood 89, № 9 (1997): 3421–33. http://dx.doi.org/10.1182/blood.v89.9.3421.

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Abstract Activated neutrophils have the ability to upregulate the expression of many genes, in particular those encoding cytokines and chemokines, and to subsequently release the corresponding proteins. Although little is known to date concerning the regulation of gene transcription in neutrophils, it is noteworthy that many of these genes depend on the activation of transcription factors, such as NF-κB, for inducible expression. We therefore investigated whether NF-κB/Rel proteins are expressed in human neutrophils, as well as their fate on cell activation. We now report that dimers consistin
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19

Gruss, HJ, D. Ulrich, SK Dower, F. Herrmann, and MA Brach. "Activation of Hodgkin cells via the CD30 receptor induces autocrine secretion of interleukin-6 engaging the NF-kappabeta transcription factor." Blood 87, no. 6 (1996): 2443–49. http://dx.doi.org/10.1182/blood.v87.6.2443.bloodjournal8762443.

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The CD30 surface molecule is a recently identified member of the tumor necrosis factor/nerve growth factor receptor superfamily. Within the cytoplasmic signal transducing domain, CD30 shares no significant homology to other members of this family. Signaling events engaged via CD30 are still unknown. We here identify the NF-kappabeta transcription factor as a target of the CD30-induced signal pathway in Hodgkin's disease (HD) cells. Exposure of HD cells to CD30 ligand induces release of interleukin-6 (IL-6) that can be duplicated by cross-linking HD- cells to an agonistic anti-CD30 specific mon
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20

Wang, Jianguo, Shawn A. Mahmud, Peter B. Bitterman, Yuqing Huo, and Arne Slungaard. "“TF-kB”-Dependent Suppression of Agonist-Mediated Tissue Factor Induction by Histone Deacetylase Inhibitors in Human Endothelial Cells and Monocytes." Blood 108, no. 11 (2006): 1745. http://dx.doi.org/10.1182/blood.v108.11.1745.1745.

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Abstract Histone deacetylase inhibitors (HDACi) such as trichostatin A (TSA) and Sodium Butyrate (NaB) can regulate gene expression by acetylating histones and transcription factors. HDACi attenuate expression of certain NF-kB-regulated cytokines, including TNF-α, IL-1β, IL-6, and IFN-γ in some inflammatory disease models. Human tissue fatctor (TF) expression is, in part, governed by a unique, NF-kB-related “TF-kB” promoter binding site. We hypothesized that HDACi would inhibit induction of TF expression by physiologic agonists. We assessed the effect of TSA and NaB upon TF expression in human
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21

Mori, Naoki, Akihiro Wada, Toshiya Hirayama, Thomas P. Parks, Christian Stratowa та Naoki Yamamoto. "Activation of Intercellular Adhesion Molecule 1 Expression by Helicobacter pylori Is Regulated by NF-κB in Gastric Epithelial Cancer Cells". Infection and Immunity 68, № 4 (2000): 1806–14. http://dx.doi.org/10.1128/iai.68.4.1806-1814.2000.

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ABSTRACT Interactions between leukocytes and epithelial cells may play a key role in Helicobacter pylori-associated gastric mucosal inflammation. This process is mediated by various cell adhesion molecules. The present study examined the molecular mechanisms leading to H. pylori-induced epithelial cell intercellular adhesion molecule-1 (ICAM-1; also called CD54) expression. Coculture of epithelial cells with cytotoxin-associated gene pathogenicity island-positive (cag PAI+) H. pylori strains, but not with a cag PAI−strain or H. pylori culture supernatants, resulted in upregulation of steady-st
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22

Ito, Noriko, Yuai Li, Tsuneo Suzuki, Daniel J. Stechschulte та Kottarappat N. Dileepan. "Transient degradation of NF-κB proteins in macrophages after interaction with mast cell granules". Mediators of Inflammation 7, № 6 (1998): 397–407. http://dx.doi.org/10.1080/09629359890776.

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The exposure of the macrophage cell line, J774 to mast cell granules (MCG) led to the form ation of altered nuclear transcription factor proteins (NFκBx), which had faster electrophoretic mobility than the p50 homodimer of NF-κB, but retained comparable DNA binding capacity. Antibodies to N-terminal peptides of p50, p52, p65 or c-Rel supershifted only a fraction of NF-κBx. Western blot analyses revealed that nuclear p65 and c-Rel were progressively degraded after exposure to MCG, whereas nuclear p50 appeared to be unaffected. In contrast, cytoplasmic p50, p65, c-Rel as well as IkBα remained in
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23

Ramezani-Rad, Parham, Huimin Geng, Lai N. Chan, et al. "SOX4 enables Oncogenic Survival Signals in Acute Lymphoblastic Leukemia." Blood 120, no. 21 (2012): 863. http://dx.doi.org/10.1182/blood.v120.21.863.863.

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Abstract Abstract 863 Background: The SOX4 (SRY-related HMG-box) transcription factor is expressed in early B- and T- cell development. In the absence of SOX4, B cell development is arrested at the pro-B to pre-B cell transition. In Sox4−/− mice, pro-B cells fail to proliferate in response to IL7 and to expand and differentiate past the pre-B cell receptor checkpoint. Interestingly, SOX4 functions a transcription factor yet closely interacts with membrane-proximal cytokine receptor signaling. The PDZ domain-containing adaptor protein syntenin (SDCBP) recruits the Sox4 protein directly to the c
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24

Hernáez, Bruno, Teresa Tarragó, Ernest Giralt, Jose M. Escribano, and Covadonga Alonso. "Small Peptide Inhibitors Disrupt a High-Affinity Interaction between Cytoplasmic Dynein and a Viral Cargo Protein." Journal of Virology 84, no. 20 (2010): 10792–801. http://dx.doi.org/10.1128/jvi.01168-10.

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ABSTRACT Several viruses target the microtubular motor system in early stages of the viral life cycle. African swine fever virus (ASFV) protein p54 hijacks the microtubule-dependent transport by interaction with a dynein light chain (DYNLL1/DLC8). This was shown to be a high-affinity interaction, and the residues gradually disappearing were mapped on DLC8 to define a putative p54 binding surface by nuclear magnetic resonance (NMR) spectroscopy. The potential of short peptides targeting the binding domain to disrupt this high-affinity protein-protein interaction was assayed, and a short peptide
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25

Sakashita, Eiji, Sawako Tatsumi, Dieter Werner, Hitoshi Endo, and Akila Mayeda. "Human RNPS1 and Its Associated Factors: a Versatile Alternative Pre-mRNA Splicing Regulator In Vivo." Molecular and Cellular Biology 24, no. 3 (2004): 1174–87. http://dx.doi.org/10.1128/mcb.24.3.1174-1187.2004.

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ABSTRACT Human RNPS1 was originally purified and characterized as a pre-mRNA splicing activator, and its role in the postsplicing process has also been proposed recently. To search for factors that functionally interact with RNPS1, we performed a yeast two-hybrid screen with a human cDNA library. Four factors were identified: p54 (also called SRp54; a member of the SR protein family), human transformer 2β (hTra2β; an exonic splicing enhancer-binding protein), hLucA (a potential component of U1 snRNP), and pinin (also called DRS and MemA; a protein localized in nuclear speckles). The N-terminal
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26

Alonso, Covadonga, James Miskin, Bruno Hernáez, et al. "African Swine Fever Virus Protein p54 Interacts with the Microtubular Motor Complex through Direct Binding to Light-Chain Dynein." Journal of Virology 75, no. 20 (2001): 9819–27. http://dx.doi.org/10.1128/jvi.75.20.9819-9827.2001.

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ABSTRACT Dynein is a minus-end-directed microtubule-associated motor protein involved in cargo transport in the cytoplasm. African swine fever virus (ASFV), a large DNA virus, hijacks the microtubule motor complex cellular transport machinery during virus infection of the cell through direct binding of virus protein p54 to the light chain of cytoplasmic dynein (LC8). Interaction of p54 and LC8 occurs both in vitro and in cells, and the two proteins colocalize at the microtubular organizing center during viral infection. p50/dynamitin, a dominant-negative inhibitor of dynein-dynactin function,
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27

Fischer, Melissa A., Sharon Friedlander, Leah Hogdal, et al. "Combination of Selective Inhibitor of Nuclear Export (SINE) Compounds, Selinexor and KPT-8602, with Venetoclax (ABT-199) Displays Enhanced Activity in Leukemia and Large Cell Lymphoma." Blood 128, no. 22 (2016): 3949. http://dx.doi.org/10.1182/blood.v128.22.3949.3949.

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Abstract Introduction: Exportin 1 (XPO1) is a well characterized and essential nucleo-cytoplasmic transport protein in the karyopherin family, and is responsible for the nuclear export of over 200 cargo proteins, including the major tumor suppressor proteins (TSPs) p53, p21, FOXO and the translation regulator elF4E. XPO1 is overexpressed in numerous cancer types including solid and hematological malignancies, often correlating with poor prognosis. Recently, a novel class of Selective Inhibitors of Nuclear Export (SINE) compounds, selinexor (KPT-330) and the second generation KPT-8602, have bee
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28

Liu, Xiaowen, Beatriu Reig, Ilya M. Nasrallah, and Patrick J. Stover. "Human Cytoplasmic Serine Hydroxymethyltransferase Is an mRNA Binding Protein†." Biochemistry 39, no. 38 (2000): 11523–31. http://dx.doi.org/10.1021/bi000665d.

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29

Naumovski, L., and M. L. Cleary. "The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M." Molecular and Cellular Biology 16, no. 7 (1996): 3884–92. http://dx.doi.org/10.1128/mcb.16.7.3884.

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Using the yeast two-hybrid system, we have isolated a cDNA (designated BBP, for Bcl2-binding protein) for a protein (Bbp) that interacts with Bcl2. Bbp is identical to 53BP2, a partial clone of which was previously isolated in a two-hybrid screen for proteins that interact with p53. In this study, we show that specific interactions of Bbp/53BP2 with either Bcl2 or p53 require its ankyrin repeats and SH3 domain. These interactions can be reproduced in vitro with bacterially expressed fusion proteins, and competition experiments indicate that Bcl2 prevents p53 from binding to Bbp/53BP2. BBP/53BP
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30

Hing, Zachary A., James S. Blachly, Virginia M. Goettl, Guramrit Singh, John C. Byrd, and Rosa Lapalombella. "Exploring the Role of the Recurrent Exportin 1 (XPO1/CRM1) Mutations E571G and E571K in Chronic Lymphocytic Leukemia." Blood 128, no. 22 (2016): 972. http://dx.doi.org/10.1182/blood.v128.22.972.972.

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Abstract Background Exportin 1 (XPO1/CRM1) is a critical component of the nuclear to cytoplasmic export machinery. As such, XPO1 shuttles tumor suppressor proteins (e.g. p53, IkB) out of the nucleus thereby preventing their anti-apoptotic function and contributing to enhanced proliferation. XPO1 also transports a subset of mRNAs (e.g. c-fos, IFN-alpha) by virtue of 3'-UTR AU-rich elements. XPO1 is upregulated in most hematologic malignancies, including CLL, where elevated XPO1 expression correlates with poor prognosis and resistance to therapy. To date, the role of nuclear export in CLL is poo
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31

Winstall, Eric, Martin Sadowski, Uwe Kühn, Elmar Wahle, and Alan B. Sachs. "TheSaccharomyces cerevisiaeRNA-binding Protein Rbp29 Functions in Cytoplasmic mRNA Metabolism." Journal of Biological Chemistry 275, no. 29 (2000): 21817–26. http://dx.doi.org/10.1074/jbc.m002412200.

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32

NIELSEN, Jacob, Sidsel K. ADOLPH, Ewa RAJPERT-De MEYTS, et al. "Nuclear transit of human zipcode-binding protein IMP1." Biochemical Journal 376, no. 2 (2003): 383–91. http://dx.doi.org/10.1042/bj20030943.

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The human IMPs (insulin-like growth factor II mRNA-binding proteins) belong to a vertebrate zipcode-binding protein family consisting of two RNA recognition motifs and four K homology domains and have been implicated in cytoplasmic mRNA localization, turnover and translational control. In the present study, we show that IMP1 is capable of translocating into nuclei of NIH 3T3 fibroblasts and its immunoreactivity is present in the nuclei of human spermatogenic cells. IMP1 does not contain a simple import signal, but nuclear entry was facilitated by disruption of RNA binding and cytoplasmic granu
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33

Jin, Yetao, Shelya X. Zeng, Hunjoo Lee, and Hua Lu. "MDM2 Mediates p300/CREB-binding Protein-associated Factor Ubiquitination and Degradation." Journal of Biological Chemistry 279, no. 19 (2004): 20035–43. http://dx.doi.org/10.1074/jbc.m309916200.

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We recently reported that MDM2, a negative feedback regulator of the tumor suppressor p53, inhibits p300/CREB-binding protein-associated factor (PCAF)-mediated p53 acetylation. Our further study showed that MDM2 also regulates the stability of PCAF. MDM2 ubiquitinated PCAFin vitroand in cells. PCAF ubiquitination occurred at the N terminus and in the nucleus, as the nuclear localization signal sequence-deletion mutant of MDM2, which localized in the cytoplasm and degraded p53, was unable to degrade nuclear PCAF. Restriction of PCAF in the nucleus by leptomycin B did not affect MDM2-mediated PC
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34

Marnef, Aline, Dominique Weil, and Nancy Standart. "RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor." Molecular Biology of the Cell 23, no. 1 (2012): 213–24. http://dx.doi.org/10.1091/mbc.e11-05-0415.

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The evolutionarily conserved Pat1 proteins are P-body components recently shown to play important roles in cytoplasmic gene expression control. Using human cell lines, we demonstrate that human Pat1b is a shuttling protein whose nuclear export is mediated via a consensus NES sequence and Crm1, as evidenced by leptomycin B (LMB) treatment. However, not all P-body components are nucleocytoplasmic proteins; rck/p54, Dcp1a, Edc3, Ge-1, and Xrn1 are insensitive to LMB and remain cytoplasmic in its presence. Nuclear Pat1b localizes to PML–associated foci and SC35-containing splicing speckles in a tr
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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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36

Khandjian, Edouard W. "Biology of the fragile X mental retardation protein, an RNA-binding protein." Biochemistry and Cell Biology 77, no. 4 (1999): 331–42. http://dx.doi.org/10.1139/o99-035.

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The fragile X syndrome, an X-linked disease, is the most frequent cause of inherited mental retardation. The syndrome results from the absence of expression of the FMR1 gene (fragile mental retardation 1) owing to the expansion of a CGG trinucleotide repeat located in the 5prime untranslated region of the gene and the subsequent methylation of its CpG island. The FMR1 gene product (FMRP) is a cytoplasmic protein that contains two KH domains and one RGG box, characteristics of RNA-binding proteins. FMRP is associated with mRNP complexes containing poly(A)+mRNA within actively translating polyri
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37

Nguyen-Chi, Mai, and Dominique Morello. "RNA-binding proteins, RNA granules, and gametes: is unity strength?" REPRODUCTION 142, no. 6 (2011): 803–17. http://dx.doi.org/10.1530/rep-11-0257.

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Changes in mRNA translation and degradation represent post-transcriptional processes operating during gametogenesis and early embryogenesis to ensure regulated protein synthesis. Numerous mRNA-binding proteins (RBPs) have been described in multiple animal models that contribute to the control of mRNA translation and decay during oogenesis and spermatogenesis. An emerging view from studies performed in germ cells and somatic cells is that RBPs associate with their target mRNAs in RNA–protein (or ribonucleoprotein) complexes (mRNPs) that assemble in various cytoplasmic RNA granules that communic
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Zou, Tongtong, Lan Liu, Jaladanki N. Rao та ін. "Polyamines modulate the subcellular localization of RNA-binding protein HuR through AMP-activated protein kinase-regulated phosphorylation and acetylation of importin α1". Biochemical Journal 409, № 2 (2007): 389–98. http://dx.doi.org/10.1042/bj20070860.

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Polyamines are required for maintenance of intestinal epithelial integrity, and a decrease in cellular polyamines increases the cytoplasmic levels of RNA-binding protein HuR stabilizing p53 and nucleophosmin mRNAs, thus inhibiting IEC (intestinal epithelial cell) proliferation. The AMPK (AMP-activated protein kinase), an enzyme involved in responding to metabolic stress, was recently found to be implicated in regulating the nuclear import of HuR. Here, we provide evidence showing that polyamines modulate subcellular localization of HuR through AMPK-regulated phosphorylation and acetylation of
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Muto, Akiko, Yoshihiko Sugihara, Minami Shibakawa, Kenzi Oshima, Tsukasa Matsuda, and Daita Nadano. "The mRNA-binding protein Serbp1 as an auxiliary protein associated with mammalian cytoplasmic ribosomes." Cell Biochemistry and Function 36, no. 6 (2018): 312–22. http://dx.doi.org/10.1002/cbf.3350.

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40

Smillie, David A., and John Sommerville. "RNA helicase p54 (DDX6) is a shuttling protein involved in nuclear assembly of stored mRNP particles." Journal of Cell Science 115, no. 2 (2002): 395–407. http://dx.doi.org/10.1242/jcs.115.2.395.

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Previously, we showed that an integral component of stored mRNP particles in Xenopus oocytes, Xp54, is a DEAD-box RNA helicase with ATP-dependent RNA-unwinding activity. Xp54 belongs to small family of helicases (DDX6) that associate with mRNA molecules encoding proteins required for progress through meiosis. Here we describe the nucleocytoplasmic translocation of recombinant Xp54 in microinjected oocytes and in transfected culture cells. We demonstrate that Xp54 is present in oocyte nuclei, its occurrence in both soluble and particle-bound forms and its ability to shuttle between nucleus and
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41

Deshler, James O., Martin I. Highett, Tatiana Abramson, and Bruce J. Schnapp. "A highly conserved RNA-binding protein for cytoplasmic mRNA localization in vertebrates." Current Biology 8, no. 9 (1998): 489–96. http://dx.doi.org/10.1016/s0960-9822(98)70200-3.

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42

Doller, Anke, Josef Pfeilschifter, and Wolfgang Eberhardt. "Signalling pathways regulating nucleo-cytoplasmic shuttling of the mRNA-binding protein HuR." Cellular Signalling 20, no. 12 (2008): 2165–73. http://dx.doi.org/10.1016/j.cellsig.2008.05.007.

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43

Nielsen, Finn C., Jacob Nielsen, Mette A. Kristensen, Grete Koch, and Jan Christiansen. "Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved KH domains." Journal of Cell Science 115, no. 10 (2002): 2087–97. http://dx.doi.org/10.1242/jcs.115.10.2087.

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The IGF-II mRNA-binding proteins (IMPs), which are composed of two RNA recognition motifs, (RRM) and four hnRNP K homology (KH) domains, have been implicated in subcytoplasmic localization of mRNAs during embryogenesis. The IMP family originated via two gene duplications before the divergence of vertebrates, and IMP homologues consisting of only the four KH motifs have been identified in Drosophila and Caenorhabditis elegans. Here we characterise the trafficking of GFP-IMP1 fusion proteins and determine the structural determinants for proper cytoplasmic localization. GFP-IMP1 is present in lar
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Schumacher, J. M., K. Lee, S. Edelhoff, and R. E. Braun. "Spnr, a murine RNA-binding protein that is localized to cytoplasmic microtubules." Journal of Cell Biology 129, no. 4 (1995): 1023–32. http://dx.doi.org/10.1083/jcb.129.4.1023.

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Previous studies in transgenic mice have established the importance of the 3' untranslated region (UTR) of the spermatid-specific protamine-1 (Prm-1) mRNA in its translational control during male germ cell development. To clone genes that mediate the translational repression or activation of the Prm-1 mRNA, we screened cDNA expression libraries made with RNA from pachytene spermatocytes and round spermatids, with an RNA probe corresponding to the 3' UTR of Prm-1. We obtained six independent clones that encode Spnr, a spermatid perinuclear RNA-binding protein. Spnr is a 71-kD protein that conta
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45

Gray, Nicola K., Lenka Hrabálková, Jessica P. Scanlon, and Richard W. P. Smith. "Poly(A)-binding proteins and mRNA localization: who rules the roost?" Biochemical Society Transactions 43, no. 6 (2015): 1277–84. http://dx.doi.org/10.1042/bst20150171.

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RNA-binding proteins are often multifunctional, interact with a variety of protein partners and display complex localizations within cells. Mammalian cytoplasmic poly(A)-binding proteins (PABPs) are multifunctional RNA-binding proteins that regulate multiple aspects of mRNA translation and stability. Although predominantly diffusely cytoplasmic at steady state, they shuttle through the nucleus and can be localized to a variety of cytoplasmic foci, including those associated with mRNA storage and localized translation. Intriguingly, PABP sub-cellular distribution can alter dramatically in respo
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Xu, Yong Zhong, Sergio Di Marco, Imed Gallouzi, Marek Rola-Pleszczynski, and Danuta Radzioch. "RNA-Binding Protein HuR Is Required for Stabilization of SLC11A1 mRNA and SLC11A1 Protein Expression." Molecular and Cellular Biology 25, no. 18 (2005): 8139–49. http://dx.doi.org/10.1128/mcb.25.18.8139-8149.2005.

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ABSTRACT The solute carrier family 11 member 1 (SLC11A1, formerly NRAMP1) gene is associated with infectious and autoimmune diseases and plays an important role in macrophage activation. Human SLC11A1 mRNA contains an AU-rich element (ARE) within the 3′ untranslated region; however, its role in the regulation of SLC11A1 gene expression has not been elucidated. Here we analyze the expression of SLC11A1 in human monocytes and HL-60 cells and then use HL-60 cells as a model to determine whether RNA-binding protein HuR is associated with the ARE and involved in SLC11A1 mRNA turnover. Our results d
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47

Babic, Ivan, Shalini Sharma, and Douglas L. Black. "A Role for Polypyrimidine Tract Binding Protein in the Establishment of Focal Adhesions." Molecular and Cellular Biology 29, no. 20 (2009): 5564–77. http://dx.doi.org/10.1128/mcb.00590-09.

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ABSTRACT Polypyrimidine tract binding protein (PTB) is a widely expressed RNA binding protein. In the nucleus PTB regulates the splicing of alternative exons, while in the cytoplasm it can affect mRNA stability, translation, and localization. Here we demonstrate that PTB transiently localizes to the cytoplasm and to protrusions in the cellular edge of mouse embryo fibroblasts during adhesion to fibronectin and the early stages of cell spreading. This cytoplasmic PTB is associated with transcripts encoding the focal adhesion scaffolding proteins vinculin and alpha-actinin 4. We demonstrate that
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48

Zhuang, Yonghua, Heather M. Berens-Norman, J. Smith Leser, Penny Clarke, and Kenneth L. Tyler. "Mitochondrial p53 Contributes to Reovirus-Induced Neuronal Apoptosis and Central Nervous System Injury in a Mouse Model of Viral Encephalitis." Journal of Virology 90, no. 17 (2016): 7684–91. http://dx.doi.org/10.1128/jvi.00583-16.

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ABSTRACTThe tumor suppressor p53 plays a critical part in determining cell fate both as a regulator of the transcription of several proapoptotic genes and through its binding interactions with Bcl-2 family proteins at mitochondria. We now demonstrate that p53 protein levels are increased in infected brains during reovirus encephalitis. This increase occurs in the cytoplasm of reovirus-infected neurons and is associated with the activation of caspase 3. Increased levels of p53 in reovirus-infected brains are not associated with increased expression levels of p53 mRNA, suggesting that p53 regula
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Singh, Nimisha, Günter Blobel, and Hang Shi. "Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport." Proceedings of the National Academy of Sciences 112, no. 1 (2014): 142–47. http://dx.doi.org/10.1073/pnas.1423194112.

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The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40–100 nt in length, known as “zipcode.” Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and
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Smith, Richard W. P., and Nicola K. Gray. "Poly(A)-binding protein (PABP): a common viral target." Biochemical Journal 426, no. 1 (2010): 1–12. http://dx.doi.org/10.1042/bj20091571.

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Cytoplasmic PABP [poly(A)-binding protein] is a multifunctional protein with well-studied roles in mRNA translation and stability. In the present review, we examine recent evidence that the activity of PABP is altered during infection with a wide range of viruses, bringing about changes in its stability, complex formation and intracellular localization. Targeting of PABP by both RNA and DNA viruses highlights the role of PABP as a central regulator of gene expression.
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