Nemo is an inducible antagonist of Wingless signaling during<i>Drosophila</i>wing development

Zeng, Yi Arial; Verheyen, Esther M.

doi:10.1242/dev.01177

Cited by 52 publications

(63 citation statements)

References 68 publications

(88 reference statements)

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“…Ectopic expression of Nemo using the Gal4-UAS system causes a number of different wing phenotypes (Brand and Perrimon, 1993;Mirkovic et al, 2002;Verheyen et al, 2001;Zeng and Verheyen, 2004). Expression of nmo with omb-Gal4 resulted in a narrowing of the regions between longitudinal veins, notably L2 and L3 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The following fly strains were used: nmo DB24 (Zeng and Verheyen, 2004), nmo adk1 and UAS-nmo C5-1e (Verheyen et al, 2001), , nmo P also referred to as nmo-lacZ (Choi and Benzer, 1994;Zeng and Verheyen, 2004), AyGal4.25-UAS-GFP.S65T (Ito et al, 1997;Zecca et al, 1996), Ubi-GFP FRT 79D, ap-Gal4 (expressed in the dorsal wing disc compartment), dpp-Gal4 (expressed along the A/P boundary), ptc-Gal4 (expressed along the A/P boundary), vg-Gal4 (expressed along the D/V boundary), prd-Gal4 (expressed in alternating stripes in the embryo), 69B-Gal4 (expressed ubiquitously in the wing pouch), omb-Gal4 (expressed in a wide domain along the A/P axis in the wing pouch), dpp d5 , dpp hr56 , dpp hr4 , UAS-Mad, UAS-MadS25A, UAS-tkv QD (Nellen et al, 1996), UAStkv wt , UAS-sog (Yu et al, 2000), P{lacW}Dad j1E4 (Tsuneizumi et al, 1997), vg Q -lacZ, salm-lacZ, rl Sem /CyO, UAS-Sem 3-1 (Rintelen et al, 2003) and UAS-GFP.…”

Section: Fly Strainsmentioning

confidence: 99%

“…The best-characterized role for Nlk is in Wnt/Wg signaling in numerous species (Golan et al, 2004;Ishitani et al, 2003a;Ishitani et al, 1999;Kanei-Ishii et al, 2004;Meneghini et al, 1999;Rocheleau et al, 1999;Shin et al, 1999;Smit et al, 2004;Thorpe and Moon, 2004;Zeng and Verheyen, 2004). Nlk phosphorylates Tcf/Lef transcription factors and inhibits their activity.…”

Section: Introductionmentioning

confidence: 99%

“…Nlk phosphorylates Tcf/Lef transcription factors and inhibits their activity. Depending on the cellular context, Nlk either inhibits Wnt-dependent gene expression (Ishitani et al, 2003b;Ishitani et al, 1999;Zeng and Verheyen, 2004) or promotes it Rocheleau et al, 1999;Thorpe and Moon, 2004). There is increasing evidence that Nlk regulates additional HMG-domain-containing proteins, such as Xenopus Sox11 and HMG2L1 (Hyodo-Miura et al, 2002;Yamada et al, 2003), as well as other transcriptional regulators such as CBP/p300, Stat3 and Myb (Kanei-Ishii et al, 2004;Ohkawara et al, 2004;Yasuda et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

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DrosophilaNemo antagonizes BMP signaling by phosphorylation of Mad and inhibition of its nuclear accumulation

et al. 2007

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Drosophila Nemo is the founding member of the Nemo-like kinase (Nlk) family of serine/threonine protein kinases that are involved in several Wnt signal transduction pathways. Here we report a novel function for Nemo in the inhibition of bone morphogenetic protein (BMP) signaling. Genetic interaction studies demonstrate that nemo can antagonize BMP signaling and can inhibit the expression of BMP target genes during wing development. Nemo can bind to and phosphorylate the BMP effector Mad. In cell culture, phosphorylation by Nemo blocks the nuclear accumulation of Mad by promoting export of Mad from the nucleus in a kinase-dependent manner. This is the first example of the inhibition of Drosophila BMP signaling by a MAPK and represents a novel mechanism of Smad inhibition through the phosphorylation of a conserved serine residue within the MH1 domain of Mad.

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Section: Resultsmentioning

confidence: 99%

Section: Fly Strainsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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DrosophilaNemo antagonizes BMP signaling by phosphorylation of Mad and inhibition of its nuclear accumulation

et al. 2007

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“…Thus, NLK has been proposed to be a negative regulator of -catenin/Tcf controlled transcription [430]. Indeed, in human embryonic kidney 293 (HEK293) cells and the cervical epithelioid carcinoma cell line HeLa, NLK inhibits -cateninregulated target genes expression [428,431].…”

Section: The -Catenin Tcf/lef Transcription Complexmentioning

confidence: 99%

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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Synthesis and characterization of chelating resins with amino moieties and application on removal of copper(II) from EDTA complexes

Wang

2005

J of Applied Polymer Sci

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Strong-field ligands (amino moieties) are introduced into a hydrogel resin to obtain a chelating resin via inversion suspension polymerization. The characteristics of chelating copolymers are measured by using Fourier transform IR spectroscopy (FTIR), elemental analysis (EA), and scanning electron microscopy (SEM). After chelating copolymers adsorb cupric ions, the absorption peak of stretch NOH is shifted to higher frequency because of a coordination reaction from the FTIR spectra. Furthermore, the mechanism of metal complex adsorption on the chelating copolymer is that the strong-field chelating ligand decomposes the bonding of the metal complexes and recoordinates the cupric ion to a chelating polymer, which is examined via FTIR, SEM with EA, and ionic chromatography analysis. The maximum adsorption capacity of cupric ions is 1.08 mmol/g and the adsorption capacity increases with the increase of the pH of the solution. The stability constant of the Cu chelating copolymer is 10 18.72 , and it can have competition adsorption with EDTA in aqueous solution. These amino chelating copolymers can be used not only to recover metal ions but also to move anion pollution in wastewater. It is interesting that parts of the cupric ions adsorbed on the chelating copolymer are reduced into cupreous ions and/or copper atoms after electron spectroscopy for chemical analysis measurement.

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Nemo is an inducible antagonist of Wingless signaling duringDrosophilawing development

Cited by 52 publications

References 68 publications

DrosophilaNemo antagonizes BMP signaling by phosphorylation of Mad and inhibition of its nuclear accumulation

DrosophilaNemo antagonizes BMP signaling by phosphorylation of Mad and inhibition of its nuclear accumulation

Wnt/beta-Catenin Signaling and Small Molecule Inhibitors

Synthesis and characterization of chelating resins with amino moieties and application on removal of copper(II) from EDTA complexes

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