hnRNP D

2006 ◽  
Author(s):  
Gary Brewer ◽  
Sandra Chesoni
Keyword(s):  
Hnrnp D

Two separate regions essential for nuclear import of the hnRNP D nucleocytoplasmic shuttling sequence

FEBS Journal ◽  
2005 ◽  
Vol 272 (15) ◽  
pp. 3975-3987 ◽  
Author(s):  
Maiko Suzuki ◽  
Megumi Iijima ◽  
Akira Nishimura ◽  
Yusuke Tomozoe ◽  
Daisuke Kamei ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Nucleocytoplasmic Shuttling ◽  
Hnrnp D

scholarly journals Circadian Amplitude of Cryptochrome 1 Is Modulated by mRNA Stability Regulation via Cytoplasmic hnRNP D Oscillation

2009 ◽  
Vol 30 (1) ◽  
pp. 197-205 ◽  
Author(s):  
Kyung-Chul Woo ◽  
Dae-Cheong Ha ◽  
Kyung-Ha Lee ◽  
Do-Yeon Kim ◽  
Tae-Don Kim ◽  
...  
Keyword(s):  
Circadian Rhythm ◽  
Mrna Stability ◽  
Posttranscriptional Regulation ◽  
Rna Binding ◽  
Clock Genes ◽  
Oscillation Amplitude ◽  
Middle Part ◽  
Peripheral Tissues ◽  
Hnrnp D ◽  
Cryptochrome 1

ABSTRACT The mammalian circadian rhythm is observed not only at the suprachiasmatic nucleus, a master pacemaker, but also throughout the peripheral tissues. Its conserved molecular basis has been thought to consist of intracellular transcriptional feedback loops of key clock genes. However, little is known about posttranscriptional regulation of these genes. In the present study, we investigated the role of the 3′-untranslated region (3′UTR) of the mouse cryptochrome 1 (mcry1) gene at the posttranscriptional level. Mature mcry1 mRNA has a 610-nucleotide 3′UTR and mediates its own degradation. The middle part of the 3′UTR contains a destabilizing cis-acting element. The deletion of this element led to a dramatic increase in mRNA stability, and heterogeneous nuclear ribonucleoprotein D (hnRNP D) was identified as an RNA binding protein responsible for this effect. Cytoplasmic hnRNP D levels displayed a pattern that was reciprocal to the mcry1 oscillation. Knockdown of hnRNP D stabilized mcry1 mRNA and resulted in enhancement of the oscillation amplitude and a slight delay of the phase. Our results suggest that hnRNP D plays a role as a fine regulator contributing to the mcry1 mRNA turnover rate and the modulation of circadian rhythm.

scholarly journals Suppression of HPV-16 late L1 5′-splice site SD3632 by binding of hnRNP D proteins and hnRNP A2/B1 to upstream AUAGUA RNA motifs

2013 ◽  
Vol 41 (22) ◽  
pp. 10488-10508 ◽  
Author(s):  
Xiaoze Li ◽  
Cecilia Johansson ◽  
Jacob Glahder ◽  
Ann-Kristin Mossberg ◽  
Stefan Schwartz
Keyword(s):  
Splice Site ◽  
Rna Motifs ◽  
Hpv 16 ◽  
Hnrnp D

Regulation of soluble Flt-1 (VEGFR-1) production by hnRNP D and protein arginine methylation

2016 ◽  
Vol 413 (1-2) ◽  
pp. 155-164 ◽  
Author(s):  
Takayuki Ikeda ◽  
Yasuo Yoshitomi ◽  
Hidehito Saito ◽  
Takeo Shimasaki ◽  
Hideki Yamaya ◽  
...  
Keyword(s):  
Arginine Methylation ◽  
Hnrnp D ◽  
Protein Arginine Methylation

hnRNP D

2012 ◽  
pp. 871-871
Author(s):  
Ryo Iwamoto ◽  
Eisuke Mekada ◽  
Thomas G. Hofmann ◽  
Eva Krieghoff-Henning ◽  
Masaaki Kobayashi ◽  
...  
Keyword(s):  
Hnrnp D

scholarly journals AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus

RNA ◽  
2012 ◽  
Vol 18 (11) ◽  
pp. 2073-2082 ◽  
Author(s):  
N. Lee ◽  
G. Pimienta ◽  
J. A. Steitz
Keyword(s):  
Noncoding Rna ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Protein Partner ◽  
Hnrnp D ◽  
Epstein Barr ◽  
Novel Protein

scholarly journals Versatile Role for hnRNP D Isoforms in the Differential Regulation of Cytoplasmic mRNA Turnover

2001 ◽  
Vol 21 (20) ◽  
pp. 6960-6971 ◽  
Author(s):  
Nianhua Xu ◽  
Chyi-Ying A. Chen ◽  
Ann-Bin Shyu
Keyword(s):  
Mammalian Cells ◽  
Mrna Decay ◽  
Sequence Similarity ◽  
Class Ii ◽  
Negative Regulator ◽  
Mrna Turnover ◽  
Dependent Manner ◽  
Coding Region ◽  
Hnrnp D

ABSTRACT An important emerging theme is that heterogeneous nuclear ribonucleoproteins (hnRNPs) not only function in the nucleus but also control the fates of mRNAs in the cytoplasm. Here, we show that hnRNP D plays a versatile role in cytoplasmic mRNA turnover by functioning as a negative regulator in an isoform-specific and cell-type-dependent manner. We found that hnRNP D discriminates among the three classes of AU-rich elements (AREs), most effectively blocking rapid decay directed by class II AREs found in mRNAs encoding cytokines. Our experiments identified the overlapping AUUUA motifs, one critical characteristic of class II AREs, to be the key feature recognized in vivo by hnRNP D for its negative effect on ARE-mediated mRNA decay. The four hnRNP D isoforms, while differing in their ability to block decay of ARE-containing mRNAs, all potently inhibited mRNA decay directed by another mRNA cis element that shares no sequence similarity with AREs, the purine-rich c-fosprotein-coding region determinant of instability. Further experiments indicated that different mechanisms underlie the inhibitory effect of hnRNP D on the two distinct mRNA decay pathways. Our study identifies a potential mechanism by which cytoplasmic mRNA turnover can be differentially and selectively regulated by hnRNP D isoforms in mammalian cells. Our results support the notion that hnRNP D serves as a key factor broadly involved in general mRNA decay.

scholarly journals RNA-Binding Protein hnRNP D Modulates Internal Ribosome Entry Site-Dependent Translation of Hepatitis C Virus RNA

2008 ◽  
Vol 82 (24) ◽  
pp. 12082-12093 ◽  
Author(s):  
Ki Young Paek ◽  
Chon Saeng Kim ◽  
Sung Mi Park ◽  
Jong Heon Kim ◽  
Sung Key Jang
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Mammalian Cells ◽  
Rna Binding ◽  
Ribosome Profiling ◽  
Hcv Rna ◽  
Entry Site ◽  
Nontranslated Region ◽  
Hnrnp D ◽  
Hcv Ires

ABSTRACT Hepatitis C virus (HCV) is one of the major causative agents of virus-related hepatitis, liver cirrhosis, and hepatocellular carcinoma in humans. Translation of the HCV polyprotein is mediated by an internal ribosomal entry site (IRES) in the 5′ nontranslated region of the genome. Here, we report that a cellular protein, hnRNP D, interacts with the 5′ border of HCV IRES (stem-loop II) and promotes translation of HCV mRNA. Overexpression of hnRNP D in mammalian cells enhances HCV IRES-dependent translation, whereas knockdown of hnRNP D with small interfering RNAs (siRNAs) inhibits translation. In addition, sequestration of hnRNP D with an interacting DNA oligomer inhibits the translation of HCV mRNA in an in vitro system. Ribosome profiling experiments reveal that HCV RNA is redistributed from heavy to light polysome fractions upon suppression of the hnRNP D level using specific siRNA. These results collectively suggest that hnRNP D plays an important role in the translation of HCV mRNA through interactions with the IRES. Moreover, knockdown of hnRNP D with siRNA significantly hampers infection by HCV. A potential role of hnRNP D in HCV proliferation is discussed.

scholarly journals Identification of 40LoVe, a Xenopus hnRNP D Family Protein Involved in Localizing a TGF-β-Related mRNA during Oogenesis

2005 ◽  
Vol 8 (4) ◽  
pp. 505-515 ◽  
Author(s):  
Kevin Czaplinski ◽  
Thomas Köcher ◽  
Malgorzata Schelder ◽  
Alexandra Segref ◽  
Matthias Wilm ◽  
...  
Keyword(s):  
Family Protein ◽  
Hnrnp D
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