Faculty Opinions recommendation of The stargazin-related protein gamma 7 interacts with the mRNA-binding protein heterogeneous nuclear ribonucleoprotein A2 and regulates the stability of specific mRNAs, including CaV2.2.

2008 ◽  
Author(s):  
Johannes Hell
Keyword(s):  
Binding Protein ◽  
Related Protein ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Mrna Binding Protein ◽  
Specific Mrnas ◽  
The Stability ◽  
Nuclear Ribonucleoprotein ◽  
Mrna Binding

scholarly journals Cytoplasmic Relocalization of Heterogeneous Nuclear Ribonucleoprotein A1 Controls Translation Initiation of Specific mRNAs

2007 ◽  
Vol 18 (12) ◽  
pp. 5048-5059 ◽  
Author(s):  
Anne Cammas ◽  
Frédéric Pileur ◽  
Sophie Bonnal ◽  
Stephen M. Lewis ◽  
Nicolas Lévêque ◽  
...  
Keyword(s):  
Hnrnp A1 ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Mrna Metabolism ◽  
Direct Demonstration ◽  
Specific Mrnas ◽  
Regulate Protein ◽  
Nuclear Ribonucleoprotein ◽  
Mrna Binding

Heterogeneous nuclear ribonucleoprotein (hnRNP) A1 is a nucleocytoplasmic shuttling protein that regulates gene expression through its action on mRNA metabolism and translation. The cytoplasmic redistribution of hnRNP A1 is a regulated process during viral infection and cellular stress. Here, we show that hnRNP A1 is an internal ribosome entry site (IRES) trans-acting factor that binds specifically to the 5′ untranslated region of both the human rhinovirus-2 and the human apoptotic peptidase activating factor 1 (apaf-1) mRNAs, thereby regulating their translation. Furthermore, the cytoplasmic redistribution of hnRNP A1 after rhinovirus infection leads to enhanced rhinovirus IRES-mediated translation, whereas the cytoplasmic relocalization of hnRNP A1 after UVC irradiation limits the UVC-triggered translational activation of the apaf-1 IRES. Therefore, this study provides a direct demonstration that IRESs behave as translational enhancer elements regulated by specific trans-acting mRNA binding proteins in given physiological conditions. Our data highlight a new way to regulate protein synthesis in eukaryotes through the subcellular relocalization of a nuclear mRNA-binding protein.

scholarly journals Neuron-Specific IMP2 Overexpression by Synapsin Promoter-Driven AAV9: A Tool to Study Its Role in Axon Regeneration

Cells ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2654
Author(s):  
Sarah Blizard ◽  
Danielle Park ◽  
Natalie O’Toole ◽  
Sheeva Norooz ◽  
Martin Dela Torre ◽  
...  
Keyword(s):  
Viral Vectors ◽  
Axon Regeneration ◽  
Viral Vector ◽  
Binding Protein ◽  
Factor Ii ◽  
Mrna Binding Protein ◽  
Specific Mrnas ◽  
Mrna Binding

Insulin-like growth factor II mRNA-binding protein (IMP) 2 is one of the three homologues (IMP1-3) that belong to a conserved family of mRNA-binding proteins. Its alternative splice product is aberrantly expressed in human hepatocellular carcinoma, and it is therefore identified as HCC. Previous works have indicated that IMP1/ZBP1 (zipcode binding protein) is critical in axon guidance and regeneration by regulating localization and translation of specific mRNAs. However, the role of IMP2 in the nervous system is largely unknown. We used the synapsin promoter-driven adeno-associated viral (AAV) 9 constructs for transgene expression both in vitro and in vivo. These viral vectors have proven to be effective to transduce the neuron-specific overexpression of IMP2 and HCC. Applying this viral vector in the injury-conditioned dorsal root ganglion (DRG) culture demonstrates that overexpression of IMP2 significantly inhibits axons regenerating from the neurons, whereas overexpression of HCC barely interrupts the process. Quantitative analysis of binding affinities of IMPs to β-actin mRNA reveals that it is closely associated with their roles in axon regeneration. Although IMPs share significant structural homology, the distinctive functions imply their different ability to localize specific mRNAs and to regulate the axonal translation.

scholarly journals Hypoxia up-regulates the activity of a novel erythropoietin mRNA binding protein.

1991 ◽  
Vol 266 (25) ◽  
pp. 16594-16598
Author(s):  
I.J. Rondon ◽  
L.A. MacMillan ◽  
B.S. Beckman ◽  
M.A. Goldberg ◽  
T. Schneider ◽  
...  
Keyword(s):  
Binding Protein ◽  
Mrna Binding Protein ◽  
Mrna Binding

scholarly journals Multiple single-stranded cis elements are associated with activated chromatin of the human c-myc gene in vivo.

1996 ◽  
Vol 16 (6) ◽  
pp. 2656-2669 ◽  
Author(s):  
G A Michelotti ◽  
E F Michelotti ◽  
A Pullner ◽  
R C Duncan ◽  
D Eick ◽  
...  
Keyword(s):  
Binding Protein ◽  
Single Strand ◽  
Upstream Sequence ◽  
Cis Elements ◽  
Sequence Element ◽  
S1 Nuclease ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Myc Gene ◽  
Nuclear Ribonucleoprotein

Transcription activation and repression of eukaryotic genes are associated with conformational and topological changes of the DNA and chromatin, altering the spectrum of proteins associated with an active gene. Segments of the human c-myc gene possessing non-B structure in vivo located with enzymatic and chemical probes. Sites hypertensive to cleavage with single-strand-specific S1 nuclease or the single-strand-selective agent potassium permanganate included the major promoters P1 and P2 as well as the far upstream sequence element (FUSE) and CT elements, which bind, respectively, the single-strand-specific factors FUSE-binding protein and heterogeneous nuclear ribonucleoprotein K in vitro. Active and inactive c-myc genes yielded different patterns of S1 nuclease and permanganate sensitivity, indicating alternative chromatin configurations of active and silent genes. The melting of specific cis elements of active c-myc genes in vivo suggested that transcriptionally associated torsional strain might assist strand separation and facilitate factor binding. Therefore, the interaction of FUSE-binding protein and heterogeneous nuclear ribonucleoprotein K with supercoiled DNA was studied. Remarkably, both proteins recognize their respective elements torsionally strained but not as liner duplexes. Single-strand- or supercoil-dependent gene regulatory proteins may directly link alterations in DNA conformation and topology with changes in gene expression.

scholarly journals Heterogeneous Nuclear Ribonucleoprotein (hnRNP) E1 Binds to hnRNP A2 and Inhibits Translation of A2 Response Element mRNAs

2006 ◽  
Vol 17 (8) ◽  
pp. 3521-3533 ◽  
Author(s):  
Linda D. Kosturko ◽  
Michael J. Maggipinto ◽  
George Korza ◽  
Joo Won Lee ◽  
John H. Carson ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
In Vitro Translation ◽  
Dependent Manner ◽  
Response Element ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Nuclear Ribonucleoprotein ◽  
Hnrnp E1

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 A2-dependent manner. hnRNP E1 is colocalized with hnRNP A2 and A2RE mRNA in granules in dendrites of oligodendrocytes. Overexpression of hnRNP E1 or microinjection of exogenous hnRNP E1 in neural cells inhibits translation of A2RE mRNA, but not of non-A2RE RNA. Excess hnRNP E1 added to an in vitro translation system reduces translation efficiency of A2RE mRNA, but not of nonA2RE RNA, in an hnRNP A2-dependent manner. These results are consistent with a model where hnRNP E1 recruited to A2RE RNA granules by binding to hnRNP A2 inhibits translation of A2RE RNA during granule transport.

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