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Rasputin protein

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https://www.readbyqxmd.com/read/26410532/crystal-structure-of-the-g3bp2-ntf2-like-domain-in-complex-with-a%C3%A2-canonical-fgdf-motif-peptide
#1
Ole Kristensen
The crystal structure of the NTF2-like domain of the human Ras GTPase SH3 Binding Protein (G3BP), isoform 2, was determined at a resolution of 2.75 Å in complex with a peptide containing a FGDF sequence motif. The overall structure of the protein is highly similar to the homodimeric N-terminal domains of the G3BP1 and Rasputin proteins. Recently, a subset of G3BP interacting proteins was recognized to share a common sequence motif, FGDF. The most studied binding partners, USP10 and viral nsP3, interfere with essential G3BP functions related to assembly of cellular stress granules...
November 6, 2015: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/26384002/mosquito-rasputin-interacts-with-chikungunya-virus-nsp3-and-determines-the-infection-rate-in-aedes-albopictus
#2
Jelke J Fros, Corinne Geertsema, Karima Zouache, Jim Baggen, Natalia Domeradzka, Daniël M van Leeuwen, Jacky Flipse, Just M Vlak, Anna-Bella Failloux, Gorben P Pijlman
BACKGROUND: Chikungunya virus (CHIKV) is an arthritogenic alphavirus (family Togaviridae), transmitted by Aedes species mosquitoes. CHIKV re-emerged in 2004 with multiple outbreaks worldwide and recently reached the Americas where it has infected over a million individuals in a rapidly expanding epidemic. While alphavirus replication is well understood in general, the specific function (s) of non-structural protein nsP3 remain elusive. CHIKV nsP3 modulates the mammalian stress response by preventing stress granule formation through sequestration of G3BP...
2015: Parasites & Vectors
https://www.readbyqxmd.com/read/24069162/rasputin-functions-as-a-positive-regulator-of-orb-in-drosophila-oogenesis
#3
Alexandre Costa, Cecilia Pazman, Kristina S Sinsimer, Li Chin Wong, Ian McLeod, John Yates, Susan Haynes, Paul Schedl
The determination of cell fate and the establishment of polarity axes during Drosophila oogenesis depend upon pathways that localize mRNAs within the egg chamber and control their on-site translation. One factor that plays a central role in regulating on-site translation of mRNAs is Orb. Orb is a founding member of the conserved CPEB family of RNA-binding proteins. These proteins bind to target sequences in 3' UTRs and regulate mRNA translation by modulating poly(A) tail length. In addition to controlling the translation of axis-determining mRNAs like grk, fs(1)K10, and osk, Orb protein autoregulates its own synthesis by binding to orb mRNA and activating its translation...
2013: PloS One
https://www.readbyqxmd.com/read/23874212/the-rna-binding-proteins-fmr1-rasputin-and-caprin-act-together-with-the-uba-protein-lingerer-to-restrict-tissue-growth-in-drosophila-melanogaster
#4
Roland Baumgartner, Hugo Stocker, Ernst Hafen
Appropriate expression of growth-regulatory genes is essential to ensure normal animal development and to prevent diseases like cancer. Gene regulation at the levels of transcription and translational initiation mediated by the Hippo and Insulin signaling pathways and by the TORC1 complex, respectively, has been well documented. Whether translational control mediated by RNA-binding proteins contributes to the regulation of cellular growth is less clear. Here, we identify Lingerer (Lig), an UBA domain-containing protein, as growth suppressor that associates with the RNA-binding proteins Fragile X mental retardation protein 1 (FMR1) and Caprin (Capr) and directly interacts with and regulates the RNA-binding protein Rasputin (Rin) in Drosophila melanogaster...
July 2013: PLoS Genetics
https://www.readbyqxmd.com/read/22414690/crystal-structure-of-the-rasputin-ntf2-like-domain-from-drosophila-melanogaster
#5
Tina Vognsen, Ole Kristensen
The crystal structure of the NTF2-like domain of the Drosophila homolog of Ras GTPase SH3 Binding Protein (G3BP), Rasputin, was determined at 2.7Å resolution. The overall structure is highly similar to nuclear transport factor 2: It is a homodimer comprised of a β-sheet and three α-helices forming a cone-like shape. However, known binding sites for RanGDP and FxFG containing peptides show electrostatic and steric differences compared to nuclear transport factor 2. A HEPES molecule bound in the structure suggests a new, and possibly physiologically relevant, ligand binding site...
March 30, 2012: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/18684830/different-types-of-nsp3-containing-protein-complexes-in-sindbis-virus-infected-cells
#6
Rodion Gorchakov, Natalia Garmashova, Elena Frolova, Ilya Frolov
Alphaviruses represent a serious public health threat and cause a wide variety of diseases, ranging from severe encephalitis, which can result in death or neurological sequelae, to mild infection, characterized by fever, skin rashes, and arthritis. In the infected cells, alphaviruses express only four nonstructural proteins, which function in the synthesis of virus-specific RNAs and in modification of the intracellular environment. The results of our study suggest that Sindbis virus (SINV) infection in BHK-21 cells leads to the formation of at least two types of nsP3-containing complexes, one of which was found in association with the plasma membrane and endosome-like vesicles, while the second was coisolated with cell nuclei...
October 2008: Journal of Virology
https://www.readbyqxmd.com/read/15602692/rasputin-more-promiscuous-than-ever-a-review-of-g3bp
#7
REVIEW
Katharine Irvine, Renee Stirling, David Hume, Derek Kennedy
In this review, we highlight what G3BP's domain structure initially suggested; that G3BPs are "scaffolding" proteins linking signal transduction to RNA metabolism. Whilst it is most attractive to hypothesise about G3BP's role in signalling to mRNA metabolism, it is not known whether all G3BP functions impinge on their RNA-binding activities, so any theories are naturally subject to this qualification. It is hypothesised that, in coordination with an array of other proteins, G3BP, in a phosphorylation-dependent manner, is involved in the post-transcriptional regulation of a subset of mRNAs, at least some of which are in common with those regulated by Hu proteins...
December 2004: International Journal of Developmental Biology
https://www.readbyqxmd.com/read/12183358/the-rasputin-effect
#8
REVIEW
Benjamin Boettner, Linda Van Aelst
No abstract text is available yet for this article.
August 15, 2002: Genes & Development
https://www.readbyqxmd.com/read/10725247/rasputin-the-drosophila-homologue-of-the-rasgap-sh3-binding-protein-functions-in-ras-and-rho-mediated-signaling
#9
C Pazman, C A Mayes, M Fanto, S R Haynes, M Mlodzik
The small GTPase Ras plays an important role in many cellular signaling processes. Ras activity is negatively regulated by GTPase activating proteins (GAPs). It has been proposed that RasGAP may also function as an effector of Ras activity. We have identified and characterized the Drosophila homologue of the RasGAP-binding protein G3BP encoded by rasputin (rin). rin mutants are viable and display defects in photoreceptor recruitment and ommatidial polarity in the eye. Mutations in rin/G3BP genetically interact with components of the Ras signaling pathway that function at the level of Ras and above, but not with Raf/MAPK pathway components...
April 2000: Development
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