ArticleMolecular and cellular biology2002
Drosophila PDZ-GEF, a guanine nucleotide exchange factor for Rap1 GTPase, reveals a novel upstream regulatory mechanism in the mitogen-activated protein kinase signaling pathway.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 39 citations in OpenAlex.
- Rap1 regulates apical contractility to allow embryonic morphogenesis without tissue disruption and acts in part via Canoe-independent mechanisms.Molecular biology of the cell · 2023Article
- Reproductive consequences of an extra long-term sperm storage organ.BMC evolutionary biology · 2020Article
- Collective Migrations ofGenetics · 2020Review
- The PDZ-GEF Gef26 regulates synapse development and function via FasII and Rap1 at the Drosophila neuromuscular junction.Experimental cell research · 2019Article
- Rap1 GTPase promotes coordinated collective cell migration in vivo.Molecular biology of the cell · 2018Article
- The Rap activator Gef26 regulates synaptic growth and neuronal survival via inhibition of BMP signaling.Molecular brain · 2017Article
- Apical accumulation of the Sevenless receptor tyrosine kinase during Drosophila eye development is promoted by the small GTPase Rap1.Genetics · 2014Article
- Rapgef2 connects GPCR-mediated cAMP signals to ERK activation in neuronal and endocrine cells.Science signaling · 2013Article
- The Rap1 guanine nucleotide exchange factor C3G is required for preservation of larval muscle integrity in Drosophila melanogaster.PloS one · 2010Article
- Control of cell adhesion dynamics by Rap1 signaling.Current opinion in cell biology · 2009Review
- The development of germline stem cells in Drosophila.Methods in molecular biology (Clifton, N.J.) · 2008Review
- The Rap GTPase activator Drosophila PDZ-GEF regulates cell shape in epithelial migration and morphogenesis.Molecular and cellular biology · 2007Article
- Rap1 controls cell adhesion and cell motility through the regulation of myosin II.The Journal of cell biology · 2007Article
- Requirement of the Caenorhabditis elegans RapGEF pxf-1 and rap-1 for epithelial integrity.Molecular biology of the cell · 2005Article
- MKP-3 has essential roles as a negative regulator of the Ras/mitogen-activated protein kinase pathway during Drosophila development.Molecular and cellular biology · 2004Article
- The Rap1 small GTPase affects cell fate or survival and morphogenetic patterning during Drosophila melanogaster eye development.Differentiation; research in biological diversityArticle
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Authors and funding
8 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PDZ-GEF is a novel guanine nucleotide exchange factor for Rap1 GTPase. Here we isolated Drosophila melanogaster PDZ-GEF (dPDZ-GEF), which contains the all-conserved domains of mammalian and nematode PDZ-GEF including cyclic nucleotide monophosphate-binding, Ras exchange motif, PDZ, RA, and GEF domains. dPDZ-GEF loss-of-function mutants were defective in the development of various organs including eye, wing, and ovary. Many of these phenotypes are strikingly similar to the phenotype of the rolled mutant, implying that dPDZ-GEF functions upstream of the mitogen-activated protein (MAP) kinase pathway. Indeed, we found that dPDZ-GEF is specifically involved in photoreceptor cell differentiation, facilitating its neuronal fate via activation of the MAP kinase pathway. Rap1 was found to link dPDZ-GEF to the MAP kinase pathway; however, Ras was not involved in the regulation of the MAP kinase pathway by dPDZ-GEF and actually had an inhibitory function. The analyses of ovary development in dPDZ-GEF-deficient mutants also demonstrated another role of dPDZ-GEF independent of the MAP kinase signaling pathway. Collectively, our findings identify dPDZ-GEF as a novel upstream regulator of various morphogenetic pathways and demonstrate the presence of a novel, Ras-independent mechanism for activating the MAP kinase signaling pathway.
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