ArticlePLoS genetics2013
Tay bridge is a negative regulator of EGFR signalling and interacts with Erk and Mkp3 in the Drosophila melanogaster wing.
Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Developmental analysis of Spalt function in the Drosophila prothoracic gland.Development (Cambridge, England) · 2024Article
- AUTS2 Syndrome: Molecular Mechanisms and Model Systems.Frontiers in molecular neuroscience · 2022Review
- Genome-wide phenotypic RNAi screen in the Drosophila wing: phenotypic description of functional classes.G3 (Bethesda, Md.) · 2021Article
- Flying Together:International journal of molecular sciences · 2020Review
- Activation-induced substrate engagement in ERK signaling.Molecular biology of the cell · 2020Article
- Ancestry of the AUTS2 family-A novel group of polycomb-complex proteins involved in human neurological disease.PloS one · 2020Article
- Identification of an Apis cerana cerana MAP kinase phosphatase 3 gene (AccMKP3) in response to environmental stress.Cell stress & chaperones · 2019Article
- The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of the N-end Rule ligase POE/UBR4 in Drosophila.PLoS biology · 2016Article
- Genome-wide distribution of Auts2 binding localizes with active neurodevelopmental genes.Translational psychiatry · 2014Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulation of Extracellular regulated kinase (Erk) activity is a key aspect of signalling by pathways activated by extracellular ligands acting through tyrosine kinase transmembrane receptors. In this process, participate proteins with kinase activity that phosphorylate and activate Erk, as well as different phosphatases that inactivate Erk by de-phosphorylation. The state of Erk phosphorylation affects not only its activity, but also its subcellular localization, defining the repertoire of Erk target proteins, and consequently, the cellular response to Erk. In this work, we characterise Tay bridge as a novel component of the EGFR/Erk signalling pathway. Tay bridge is a large nuclear protein with a domain of homology with human AUTS2, and was previously identified due to the neuronal phenotypes displayed by loss-of-function mutations. We show that Tay bridge antagonizes EGFR signalling in the Drosophila melanogaster wing disc and other tissues, and that the protein interacts with both Erk and Mkp3. We suggest that Tay bridge constitutes a novel element involved in the regulation of Erk activity, acting as a nuclear docking for Erk that retains this protein in an inactive form in the nucleus.
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