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Journal articles on the topic 'HnRNP E1'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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1

Choi, Mie-Young. "Cloning of hnRNP E1 cDNA via yeast two-hybrid system and a study on protein-protein interaction between hnRNP E1 and hnRNP K." Journal of the Korea Academia-Industrial cooperation Society 9, no. 6 (2008): 1795–99. http://dx.doi.org/10.5762/kais.2008.9.6.1795.

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2

Kosturko, Linda D., Michael J. Maggipinto, George Korza, Joo Won Lee, John H. Carson, and Elisa Barbarese. "Heterogeneous Nuclear Ribonucleoprotein (hnRNP) E1 Binds to hnRNP A2 and Inhibits Translation of A2 Response Element mRNAs." Molecular Biology of the Cell 17, no. 8 (2006): 3521–33. http://dx.doi.org/10.1091/mbc.e05-10-0946.

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Heterogeneous nuclear ribonucleoprotein (hnRNP) A2 is a trans-acting RNA-binding protein that mediates trafficking of RNAs containing the cis-acting A2 response element (A2RE). Previous work has shown that A2RE RNAs are transported to myelin in oligodendrocytes and to dendrites in neurons. hnRNP E1 is an RNA-binding protein that regulates translation of specific mRNAs. Here, we show by yeast two-hybrid analysis, in vivo and in vitro coimmunoprecipitation, in vitro cross-linking, and fluorescence correlation spectroscopy that hnRNP E1 binds to hnRNP A2 and is recruited to A2RE RNA in an hnRNP A

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3

Mohanty, Bidyut K., Joseph AQ Karam, Breege V. Howley, et al. "Heterogeneous nuclear ribonucleoprotein E1 binds polycytosine DNA and monitors genome integrity." Life Science Alliance 4, no. 9 (2021): e202000995. http://dx.doi.org/10.26508/lsa.202000995.

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Heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) is a tumor suppressor protein that binds site- and structure-specifically to RNA sequences to regulate mRNA stability, facilitate alternative splicing, and suppress protein translation on several metastasis-associated mRNAs. Here, we show that hnRNP E1 binds polycytosine-rich DNA tracts present throughout the genome, including those at promoters of several oncogenes and telomeres and monitors genome integrity. It binds DNA in a site- and structure-specific manner. hnRNP E1-knockdown cells displayed increased DNA damage signals including γ-H

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4

Ostareck-Lederer, Antje, Dirk H. Ostareck, Christophe Cans, et al. "c-Src-Mediated Phosphorylation of hnRNP K Drives Translational Activation of Specifically Silenced mRNAs." Molecular and Cellular Biology 22, no. 13 (2002): 4535–43. http://dx.doi.org/10.1128/mcb.22.13.4535-4543.2002.

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ABSTRACT hnRNPK and hnRNP E1/E2 mediate translational silencing of cellular and viral mRNAs in a differentiation-dependent way by binding to specific regulatory sequences. The translation of 15-lipoxygenase (LOX) mRNA in erythroid precursor cells and of the L2 mRNA of human papilloma virus type 16 (HPV-16) in squamous epithelial cells is silenced when either of these cells is immature and is activated in maturing cells by unknown mechanisms. Here we address the question of how the silenced mRNA can be translationally activated. We show that hnRNP K and the c-Src kinase specifically interact wi

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5

Han, Sun‐Young, and Mieyoung Choi. "Human ribosomal protein L18a interacts with hnRNP E1." Animal Cells and Systems 12, no. 3 (2008): 143–48. http://dx.doi.org/10.1080/19768354.2008.9647167.

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6

Chaudhury, A., P. Chander, and P. H. Howe. "Heterogeneous nuclear ribonucleoproteins (hnRNPs) in cellular processes: Focus on hnRNP E1's multifunctional regulatory roles." RNA 16, no. 8 (2010): 1449–62. http://dx.doi.org/10.1261/rna.2254110.

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7

Brown, Andrew S., Bidyut K. Mohanty, and Philip H. Howe. "Identification and characterization of an hnRNP E1 translational silencing motif." Nucleic Acids Research 44, no. 12 (2016): 5892–907. http://dx.doi.org/10.1093/nar/gkw241.

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8

Tang, Ying-Sheng, Rehana A. Khan, Yonghua Zhang, et al. "Incrimination of Heterogeneous Nuclear Ribonucleoprotein E1 (hnRNP-E1) as a Candidate Sensor of Physiological Folate Deficiency." Journal of Biological Chemistry 286, no. 45 (2011): 39100–39115. http://dx.doi.org/10.1074/jbc.m111.230938.

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9

Ajiro, Masahiko, Shuang Tang, John Doorbar, and Zhi-Ming Zheng. "Serine/Arginine-Rich Splicing Factor 3 and Heterogeneous Nuclear Ribonucleoprotein A1 Regulate Alternative RNA Splicing and Gene Expression of Human Papillomavirus 18 through Two Functionally DistinguishablecisElements." Journal of Virology 90, no. 20 (2016): 9138–52. http://dx.doi.org/10.1128/jvi.00965-16.

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ABSTRACTHuman papillomavirus 18 (HPV18) is the second most common oncogenic HPV type associated with cervical, anogenital, and oropharyngeal cancers. Like other oncogenic HPVs, HPV18 encodes two major (one early and one late) polycistronic pre-mRNAs that are regulated by alternative RNA splicing to produce a repertoire of viral transcripts for the expression of individual viral genes. However, RNAcis-regulatory elements andtrans-acting factors contributing to HPV18 alternative RNA splicing remain unknown. In this study, an exonic splicing enhancer (ESE) in the nucleotide (nt) 3520 to 3550 regi

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10

Link, Laura A., Breege V. Howley, George S. Hussey, and Philip H. Howe. "PCBP1/HNRNP E1 Protects Chromosomal Integrity by Translational Regulation of CDC27." Molecular Cancer Research 14, no. 7 (2016): 634–46. http://dx.doi.org/10.1158/1541-7786.mcr-16-0018.

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11

Ostareck, Dirk H., Antje Ostareck-Lederer, Matthias Wilm, Bernd J. Thiele, Matthias Mann, and Matthias W. Hentze. "mRNA Silencing in Erythroid Differentiation: hnRNP K and hnRNP E1 Regulate 15-Lipoxygenase Translation from the 3′ End." Cell 89, no. 4 (1997): 597–606. http://dx.doi.org/10.1016/s0092-8674(00)80241-x.

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12

Jang, Seonghui, Heegwon Shin, Jungmin Lee, Youngmi Kim, Geunu Bak, and Younghoon Lee. "Regulation of BC200 RNA-mediated translation inhibition by hnRNP E1 and E2." FEBS Letters 591, no. 2 (2017): 393–405. http://dx.doi.org/10.1002/1873-3468.12544.

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13

Woolaway, Kathryn, Kengo Asai, Andrew Emili, and Alan Cochrane. "hnRNP E1 and E2 have distinct roles in modulating HIV-1 gene expression." Retrovirology 4, no. 1 (2007): 28. http://dx.doi.org/10.1186/1742-4690-4-28.

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14

Howley, Breege V., and Philip H. Howe. "TGF-beta signaling in cancer: post-transcriptional regulation of EMT via hnRNP E1." Cytokine 118 (June 2019): 19–26. http://dx.doi.org/10.1016/j.cyto.2017.12.032.

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15

Xiao, Suhong, Ying-Sheng Tang, Rehana A. Khan, et al. "Influence of Physiologic Folate Deficiency on Human Papillomavirus Type 16 (HPV16)-harboring Human Keratinocytes in Vitro and in Vivo." Journal of Biological Chemistry 287, no. 15 (2012): 12559–77. http://dx.doi.org/10.1074/jbc.m111.317040.

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Although HPV16 transforms infected epithelial tissues to cancer in the presence of several co-factors, there is insufficient molecular evidence that poor nutrition has any such role. Because physiological folate deficiency led to the intracellular homocysteinylation of heterogeneous nuclear ribonucleoprotein E1 (hnRNP-E1) and activated a nutrition-sensitive (homocysteine-responsive) posttranscriptional RNA operon that included interaction with HPV16 L2 mRNA, we investigated the functional consequences of folate deficiency on HPV16 in immortalized HPV16-harboring human (BC-1-Ep/SL) keratinocyte

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16

Zhao, Xiaomin, Daniel Öberg, Margaret Rush, Joanna Fay, Helen Lambkin, and Stefan Schwartz. "A 57-Nucleotide Upstream Early Polyadenylation Element in Human Papillomavirus Type 16 Interacts with hFip1, CstF-64, hnRNP C1/C2, and Polypyrimidine Tract Binding Protein." Journal of Virology 79, no. 7 (2005): 4270–88. http://dx.doi.org/10.1128/jvi.79.7.4270-4288.2005.

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ABSTRACT We have investigated the role of the human papillomavirus type 16 (HPV-16) early untranslated region (3′ UTR) in HPV-16 gene expression. We found that deletion of the early 3′ UTR reduced the utilization of the early polyadenylation signal and, as a consequence, resulted in read-through into the late region and production of late L1 and L2 mRNAs. Deletion of the U-rich 3′ half of the early 3′ UTR had a similar effect, demonstrating that the 57-nucleotide U-rich region acted as an enhancing upstream element on the early polyadenylation signal. In accordance with this, the newly identif

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17

Ostareck-Lederer, Antje, and Dirk H. Ostareck. "Precision Mechanics with Multifunctional Tools: How HnRNP K and HnRNPs E1/E2 Contribute to Post-Transcriptional Control of Gene Expression in Hematopoiesis." Current Protein & Peptide Science 13, no. 4 (2012): 391–400. http://dx.doi.org/10.2174/138920312801619484.

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18

Zhong, Nanbert, Gabriel Radu, Weina Ju, and W. Ted Brown. "Novel progerin-interactive partner proteins hnRNP E1, EGF, Mel 18, and UBC9 interact with lamin A/C." Biochemical and Biophysical Research Communications 338, no. 2 (2005): 855–61. http://dx.doi.org/10.1016/j.bbrc.2005.10.020.

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19

Ho, J. J. D., G. B. Robb, S. C. Tai, et al. "Active Stabilization of Human Endothelial Nitric Oxide Synthase mRNA by hnRNP E1 Protects against Antisense RNA and MicroRNAs." Molecular and Cellular Biology 33, no. 10 (2013): 2029–46. http://dx.doi.org/10.1128/mcb.01257-12.

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20

Chaudhury, Arindam, George S. Hussey, Partho S. Ray, Ge Jin, Paul L. Fox та Philip H. Howe. "TGF-β-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI". Nature Cell Biology 12, № 3 (2010): 286–93. http://dx.doi.org/10.1038/ncb2029.

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21

Li, Yang, and Mirko Hennig. "1H, 15N and 13C backbone resonance assignments of the N-terminal, tandem KH domains of human hnRNP E1." Biomolecular NMR Assignments 9, no. 2 (2015): 431–34. http://dx.doi.org/10.1007/s12104-015-9624-0.

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22

Tang, Ying-Sheng, Rehana A. Khan, Suhong Xiao, et al. "Evidence Favoring a Positive Feedback Loop for Physiologic Auto Upregulation of hnRNP-E1 during Prolonged Folate Deficiency in Human Placental Cells." Journal of Nutrition 147, no. 4 (2017): 482–98. http://dx.doi.org/10.3945/jn.116.241364.

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23

Reimann, Iris, Antje Huth, Holger Thiele, and Bernd-Joachim Thiele. "Suppression of 15-lipoxygenase synthesis by hnRNP E1 is dependent on repetitive nature of LOX mRNA 3′-UTR control element DICE." Journal of Molecular Biology 315, no. 5 (2002): 965–74. http://dx.doi.org/10.1006/jmbi.2001.5315.

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24

Mayanil, Chandra Shekhar K. "That Which Is Bad Can Trigger Good in the Human Body—Homocysteine-Bound hnRNP-E1 as a Molecular Sensor of Physiologic Folate Deficiency." Journal of Nutrition 147, no. 4 (2017): 471–72. http://dx.doi.org/10.3945/jn.117.247924.

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25

Howley, B. V., G. S. Hussey, L. A. Link та P. H. Howe. "Translational regulation of inhibin βA by TGFβ via the RNA-binding protein hnRNP E1 enhances the invasiveness of epithelial-to-mesenchymal transitioned cells". Oncogene 35, № 13 (2015): 1725–35. http://dx.doi.org/10.1038/onc.2015.238.

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26

Persson, Pontus B., Angela Skalweit, Ralf Mrowka, and Bernd-Joachim Thiele. "Control of renin synthesis." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 285, no. 3 (2003): R491—R497. http://dx.doi.org/10.1152/ajpregu.00101.2003.

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Studies published recently have considerably enhanced our understanding of the mechanisms controlling renin production. With regard to the control of renin transcription, two enhancer regions have been identified that markedly augment renin synthesis in cell lines. In the absence of this enhancer activity, the basic promoter of the renin gene increases transcription only two- to threefold. The location of one (Jones CA, Sigmund CD, McGowan RA, Kane-Haas CM, and Gross KW. Mol Endocrinol 4: 375-383, 1990) transcription enhancer in the mouse gene is at about -2.7 kb and in humans at roughly -11 k

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27

Zhang, Yingying, Lin Meng, Lin Xiao, Ruiwang Liu, Zhonghai Li, and Ying-lei Wang. "The RNA-Binding Protein PCBP1 Functions as a Tumor Suppressor in Prostate Cancer by Inhibiting Mitogen Activated Protein Kinase 1." Cellular Physiology and Biochemistry 48, no. 4 (2018): 1747–54. http://dx.doi.org/10.1159/000492315.

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Background/Aims: Poly r(C) binding protein (PCBP) 1 or heterogeneous ribonucleoprotein (hnRNP) E1 is a RNA binding protein functional in multiple biological processes. In prostate cancer (PCa), PCBP1 loss was shown to be involved with increased stemness in PCacells; however, the underlying mechanism remains unclear. Method: The role of PCBP1 in prostate tumor formationwas determined by xenograft assays. Immunoprecipitationand mass spectrometry were performed to find the pathways altered after PCBP1 knockdown. Cell proliferation, migration, invasion, and soft agar colony formationassays and xen

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28

Ross, A. F., Y. Oleynikov, E. H. Kislauskis, K. L. Taneja, and R. H. Singer. "Characterization of a beta-actin mRNA zipcode-binding protein." Molecular and Cellular Biology 17, no. 4 (1997): 2158–65. http://dx.doi.org/10.1128/mcb.17.4.2158.

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Localization of beta-actin mRNA to the leading edge of fibroblasts requires the presence of conserved elements in the 3' untranslated region of the mRNA, including a 54-nucleotide element which has been termed the "zipcode" (E. Kislauskis, X. Zhu, and R. H. Singer, J. Cell Biol. 127:441-451, 1994). In order to identify proteins which bind to the zipcode and possibly play a role in localization, we performed band-shift mobility assays, UV cross-linking, and affinity purification experiments. A protein of 68 kDa was identified which binds to the proximal (to the coding region) half of the zipcod

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29

Ostareck-lederer, Antje, Dirk H. Ostareck, and Matthias W. Hentze. "Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2." Trends in Biochemical Sciences 23, no. 11 (1998): 409–11. http://dx.doi.org/10.1016/s0968-0004(98)01301-2.

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30

Van Zalen, Sebastiaan, Grace R. Jeschke, Elizabeth Hexner, and J. Eric Russell. "Lineage- and Developmental Stage-Specific Patterns Of Auf-1 Isoform Expression Contribute To The Regulation Of Erythroid-Specific mRNAs." Blood 122, no. 21 (2013): 10. http://dx.doi.org/10.1182/blood.v122.21.10.10.

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Abstract Post-transcriptional events that regulate the stabilities of one or more specific mRNAs are increasingly recognized for their importance to cell development and differentiation: genome-wide analyses attribute ∼50% of changes in gene expression to alterations in the stabilities of their encoded mRNAs. Processes that differentially regulate the half-lives of mRNAs are particularly important in definitive erythropoiesis, as they control the relative levels of actively translating transcripts in the interval when the nucleus is transcriptionally silenced and is ultimately extruded. We rec

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31

Ostareck-Lederer, Antje, and Dirk H. Ostareck. "Control of mRNA translation and stability in haematopoietic cells: The function of hnRNPs K and E1/E2." Biology of the Cell 96, no. 6 (2004): 407–11. http://dx.doi.org/10.1016/j.biolcel.2004.03.010.

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32

Grelet, Simon, and Philip H. Howe. "hnRNP E1 at the crossroads of translational regulation of epithelial-mesenchymal transition." Journal of Cancer Metastasis and Treatment 2019 (March 11, 2019). http://dx.doi.org/10.20517/2394-4722.2018.85.

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33

Zheng, Yunji, Johanna Jönsson, Chengyu Hao, et al. "Heterogeneous Nuclear Ribonucleoprotein A1 (hnRNP A1) and hnRNP A2 Inhibit Splicing to Human Papillomavirus 16 Splice Site SA409 through a UAG-Containing Sequence in the E7 Coding Region." Journal of Virology 94, no. 20 (2020). http://dx.doi.org/10.1128/jvi.01509-20.

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ABSTRACT Human papillomavirus 16 (HPV16) 5′-splice site SD226 and 3′-splice site SA409 are required for production of the HPV16 E7 mRNAs, whereas unspliced mRNAs produce E6 mRNAs. The E6 and E7 proteins are essential in the HPV16 replication cycle but are also the major HPV16 proteins required for induction and maintenance of malignancy caused by HPV16 infection. Thus, a balanced expression of unspliced and spliced mRNAs is required for production of sufficient quantities of E6 and E7 proteins under physiological and pathophysiological conditions. If splicing becomes too efficient, the levels

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34

Ansa-Addo, Ephraim Abrokwa, Huai-Cheng Huang, Brian Riesenberg, et al. "RNA-Binding Protein PCBP1/hnRNP E1 is an Intracellular Checkpoint for Shaping Effector Versus Regulatory T Cells in Immunity and Cancer." SSRN Electronic Journal, 2019. http://dx.doi.org/10.2139/ssrn.3418426.

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