The trimeric G protein Go inflicts a double impact on axin in the Wnt/frizzled signaling pathway

Egger-Adam, Diane; Katanaev, Vladimir L.

doi:10.1002/dvdy.22060

Cited by 47 publications

(67 citation statements)

References 78 publications

(149 reference statements)

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“…In some cases, APC-mediated regulation of cell cycle progress appears to be independent of b-catenin-mediated signals (Ishidate et al, 2000). More recently, it was described that Gao directly acts on the axin RGS domain, which neutralizes the axin inhibitory function for Wnt signalling (Egger-Adam & Katanaev, 2010). Gao may participate in overactivation of Wnt/Fz signalling, and the interaction of Gao with Rab4 and Rab5 may be involved in Gaomediated Wnt signalling activation (Egger-Adam & Katanaev, 2008;Koval et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Axin expression enhances herpes simplex virus type 1 replication by inhibiting virus-mediated cell death in L929 cells

Choi

Kim

Jho

et al. 2013

Journal of General Virology

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Herpes simplex virus type 1 (HSV-1) replicates in various cell types and induces early cell death, which limits viral replication in certain cell types. Axin is a scaffolding protein that regulates Wnt signalling and participates in various cellular events, including cellular proliferation and cell death. The effects of axin expression on HSV-1 infection were investigated based on our initial observation that Wnt3a treatment or axin knockdown reduced HSV-1 replication. L929 cells expressed the axin protein in a doxycycline-inducible manner (L-axin) and enhanced HSV-1 replication in comparison to control cells (L-EV). HSV-1 infection induced cell death as early as 6 h after infection through the necrotic pathway and required de novo protein synthesis in L929 cells. Subsequent analysis of viral protein expression suggested that axin expression led to suppression of HSV-1-induced premature cell death, resulting in increased late gene expression. In analysis of axin deletion mutants, the regulators of the G-protein signalling (RGS) domain were involved in the axin-mediated enhancement of viral replication and reduction in cell death. These results suggest that viral replication enhancement might be mediated by the axin RGS domain.

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Section: Discussionmentioning

confidence: 99%

Axin expression enhances herpes simplex virus type 1 replication by inhibiting virus-mediated cell death in L929 cells

Choi

Kim

Jho

et al. 2013

Journal of General Virology

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“…It was shown in Drosophila that the recruitement of Dishevelled and Axin to the membrane is facilitated through G-proteins with trimeric Go-proteins acting as immediate transducer [224][225][226][227]. One of the Go subunits, G o, uses an RGS domain to interact directly with Axin, recruiting it to the membrane [54,228]. G o also interacts with Rab5, an interaction that presumuably promotes the internalization of the Wnt/Frizzled/LRP complexes [54,229].…”

Section: The Wnt Receptor Complexmentioning

confidence: 99%

“…One of the Go subunits, G o, uses an RGS domain to interact directly with Axin, recruiting it to the membrane [54,228]. G o also interacts with Rab5, an interaction that presumuably promotes the internalization of the Wnt/Frizzled/LRP complexes [54,229]. The Go subunit, G , recruits Dishevelled to the plasma membrane upon Wnt binding to the Frizzled receptors [54].…”

Section: The Wnt Receptor Complexmentioning

confidence: 99%

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Wnt/beta-Catenin Signaling and Small Molecule Inhibitors

Voronkov¹,

Krauß²

2012

CPD

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Wnt/ -catenin signaling is a branch of a functional network that dates back to the first metazoans and it is involved in a broad range of biological systems including stem cells, embryonic development and adult organs. Deregulation of components involved in Wnt/ -catenin signaling has been implicated in a wide spectrum of diseases including a number of cancers and degenerative diseases. The key mediator of Wnt signaling, -catenin, serves several cellular functions. It functions in a dynamic mode at multiple cellular locations, including the plasma membrane, where -catenin contributes to the stabilization of intercellular adhesive complexes, the cytoplasm where -catenin levels are regulated and the nucleus where -catenin is involved in transcriptional regulation and chromatin interactions. Central effectors of -catenin levels are a family of cysteine-rich secreted glycoproteins, known as Wnt morphogens. Through the LRP5/6-Frizzled receptor complex, Wnts regulate the location and activity of the destruction complex and consequently intracellularcatenin levels. However, -catenin levels and their effects on transcriptional programs are also influenced by multiple other factors including hypoxia, inflammation, hepatocyte growth factor-mediated signaling, and the cell adhesion molecule E-cadherin. The broad implications of Wnt/ -catenin signaling in development, in the adult body and in disease render the pathway a prime target for pharmacological research and development. The intricate regulation of -catenin at its various locations provides alternative points for therapeutic interventions.

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“…Wnt signaling is involved in numerous developmental processes and regulates synaptic formation and stability in the adult organism [4]. In the canonical pathway, the ligand Wnt activates the receptor Frizzled (Fz) and its co-receptor LRP5/6 to induce reorganization of the β-catenin-destruction complex, a protein complex consisting of Axin, APC, glycogen synthase kinase 3β (GSK3β, Shaggy [Sgg] in Drosophila) and casein kinase, through the scaffolding protein Dishevelled and the trimeric Go protein [4,5]. Thus Wnt signaling leads to stabilization of β-catenin and its translocation to the nucleus where it induces transcription of Wnt target genes.…”

Section: Resultsmentioning

confidence: 99%

Lack of evidence of the interaction of the Aß peptide with the Wnt signaling cascade in Drosophila models of Alzheimer¿s disease

Lüchtenborg

Katanaev

2014

Molecular Brain

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Background: Alzheimer's disease (AD) is the leading form of dementia worldwide. The Aβ-peptide is believed to be the major pathogenic compound of the disease. Since several years it is hypothesized that Aβ impacts the Wnt signaling cascade and therefore activation of this signaling pathway is proposed to rescue the neurotoxic effect of Aβ. Findings: Expression of the human Aβ42 in the Drosophila nervous system leads to a drastically shortened life span. We found that the action of Aβ42 specifically in the glutamatergic motoneurons is responsible for the reduced survival. However, we find that the morphology of the glutamatergic larval neuromuscular junctions, which are widely used as the model for mammalian central nervous system synapses, is not affected by Aβ42 expression. We furthermore demonstrate that genetic activation of the Wnt signal transduction pathway in the nervous system is not able to rescue the shortened life span or a rough eye phenotype in Drosophila.

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The trimeric G protein Go inflicts a double impact on axin in the Wnt/frizzled signaling pathway

Cited by 47 publications

References 78 publications

Axin expression enhances herpes simplex virus type 1 replication by inhibiting virus-mediated cell death in L929 cells

Axin expression enhances herpes simplex virus type 1 replication by inhibiting virus-mediated cell death in L929 cells

Wnt/beta-Catenin Signaling and Small Molecule Inhibitors

Lack of evidence of the interaction of the Aß peptide with the Wnt signaling cascade in Drosophila models of Alzheimer¿s disease

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