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GTPase activating protein

This gene encodes one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. It binds specifically to the Ras-GTPase-activating protein by associating with its SH3 domain. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: GAP, CAN, TIA, fibrillin-1, HAD
Papers on G3BP
CsTNF1, a teleost tumor necrosis factor that promotes antibacterial and antiviral immune defense in a manner that depends on the conserved receptor binding site.
Zhang et al., Qingdao, China. In Dev Comp Immunol, Feb 2016
Fish administered with rCsTNF1, but not with rCsTNF1M1 and rCsTNF1M2, exhibited enhanced expression of IL-1, IL-6, IL-8, IL-27, TLR9 and G3BP in a time-dependent manner and augmented resistance against bacterial and viral infection.
Melanoma differentiation-associated gene 5 is involved in the induction of stress granules and autophagy by protonophore CCCP.
Zhang et al., In Biol Chem, Feb 2016
Furthermore, the depletion of MDA5 or G3BP1 led to reduced autophagy in CCCP-stimulated cells, implying that the regulatory effect of MDA5 with respect to autophagy depends on its role in SG formation.
G3BP1 restricts HIV-1 replication in macrophages and T-cells by sequestering viral RNA.
Kootstra et al., Amsterdam, Netherlands. In Virology, Dec 2015
We identified GTPase-activating protein-(SH3 domain)-binding protein 1 (G3BP1) as a cellular factor that restricts HIV-1, by analyzing transcriptome profiles of in vitro-cytokine-activated macrophages that are non-permissive to HIV-1 replication.
Dengue virus infection induces formation of G3BP1 granules in human lung epithelial cells.
Zhang et al., Guangzhou, China. In Arch Virol, Dec 2015
In the current study, we further investigated SG formation in human epithelial A549 cells by detecting subcellular localization of two SG hallmarks, TIA-1 and G3BP1.
Doubly Spliced RNA of Hepatitis B Virus Suppresses Viral Transcription via TATA-Binding Protein and Induces Stress Granule Assembly.
Chang et al., Taiwan. In J Virol, Dec 2015
Immunofluorescence experiments showed that 2.2DS-RNA colocalized with cytoplasmic TBP and the stress granule components, G3BP and poly(A)-binding protein 1 (PABP1), in Huh7 cells.
Crystal structure of the G3BP2 NTF2-like domain in complex with a canonical FGDF motif peptide.
Kristensen, Copenhagen, Denmark. In Biochem Biophys Res Commun, Dec 2015
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.
Integrative Genomics-Based Discovery of Novel Regulators of the Innate Antiviral Response.
Huynen et al., Nijmegen, Netherlands. In Plos Comput Biol, Oct 2015
MAP3K11, CDK11B, PSMA3, TRIM14, HSPA9B, CDC37, NUP98, G3BP1), and include uncharacterized factors (DDX17, C6orf58, C16orf57, PKN2, SNW1).
SAMHD1 Inhibits LINE-1 Retrotransposition by Promoting Stress Granule Formation.
Guo et al., Beijing, China. In Plos Genet, Jul 2015
In support of this new mechanism of action, depletion of stress granule marker proteins G3BP1 or TIA1 abrogates stress granule formation and overcomes SAMHD1 inhibition of LINE-1.
MYCNOS functions as an antisense RNA regulating MYCN.
Morris et al., Los Angeles, United States. In Rna Biol, 2014
Here we report that MYCNOS transcripts function as a modulator of the MYCN locus, affecting MYCN promoter usage and recruiting various proteins, including the Ras GTPase-activating protein-binding protein G3BP1, to the upstream MYCN promoter.
Multiple Poliovirus Proteins Repress Cytoplasmic RNA Granules.
Lloyd et al., Houston, United States. In Viruses, 2014
Of the two forms of G3BP, only G3BP1 is cleaved by a virus proteinase, 3C(pro), whereas G3BP2 is not cleaved by 3C(pro) or 2A(pro).
Mosquito Rasputin interacts with chikungunya virus nsP3 and determines the infection rate in Aedes albopictus.
Pijlman et al., Wageningen, Netherlands. In Parasit Vectors, 2014
CHIKV nsP3 modulates the mammalian stress response by preventing stress granule formation through sequestration of G3BP.
Arginine methylation of G3BP1 in response to Wnt3a regulates β-catenin mRNA.
Malbon et al., Stony Brook, United States. In J Cell Sci, 2011
G3BP1 is a novel Ctnnb1 mRNA binding protein. Methylation of G3BP1 constitutes a molecular switch that regulates Ctnnb1 mRNA in response to Wnt3a.
The N-terminal domain of G3BP enhances cell motility and invasion by posttranscriptional regulation of BART.
Hollingsworth et al., Omaha, United States. In Mol Cancer Res, 2011
overexpression of the amino (N)-terminal region of G3BP, including the binding region for BART mRNA, dominant-negatively inhibits formation of the complex between endogenous G3BP and BART mRNA, and increases the expression of BART.
Post-transcriptional regulation of the mitochondrial H(+)-ATP synthase: a key regulator of the metabolic phenotype in cancer.
Cuezva et al., Madrid, Spain. In Biochim Biophys Acta, 2011
The role of the ATPase Inhibitor Factor 1 (IF1) and of Ras-GAP SH3 binding protein 1 (G3BP1), controlling the activity of the H(+)-ATP synthase and the translation of β-F1-ATPase mRNA respectively in cancer cells is emphasized.
Intracellular CD24 inhibits cell invasion by posttranscriptional regulation of BART through interaction with G3BP.
Hollingsworth et al., Omaha, United States. In Cancer Res, 2011
CD24 may play a role in the inhibition of cell invasion and metastasis, and that intracellular CD24 inhibits invasiveness and metastasis through its influence on the posttranscriptional regulation of BART mRNA levels via G3BP RNase activity.
Functional interaction between type III-secreted protein IncA of Chlamydophila psittaci and human G3BP1.
Hänel et al., Jena, Germany. In Plos One, 2010
interaction between IncA and G3BP1 of Hep-2 cells infected with Chlamydophila psittaci reduces c-Myc concentration
Revisiting G3BP1 as a RasGAP binding protein: sensitization of tumor cells to chemotherapy by the RasGAP 317-326 sequence does not involve G3BP1.
Widmann et al., Lausanne, Switzerland. In Plos One, 2010
arguments against G3BP1 being a genuine RasGAP-binding partner
[G3BP: a promising target for cancer therapy].
Shao et al., Beijing, China. In Yao Xue Xue Bao, 2010
G3BP (Ras-GTPase-activating protein SH3 domain binding protein), a protein which binds to RasGAP SH3 domain, belongs to RNA-binding protein family, implicating in the downstream of Ras signaling.
Rasputin, more promiscuous than ever: a review of G3BP.
Kennedy et al., Australia. In Int J Dev Biol, 2004
G3BPs are scaffolding proteins linking signal transduction to RNA metabolism (review)
Ras-GTPase activating protein (GAP): a putative effector for Ras.
Schweighoffer et al., Vitry-sur-Seine, France. In Cell Signal, 1997
The newly found GAP-SH3 domain Binding Protein (G3BP) may be one of these.
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