ArticleScientific reports2016
Distinct Biochemical Activities of Eyes absent During Drosophila Eye Development.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Modulating the levels and activity of the retinal determination network is sufficient to induce the specification of distinct tissue fates in Drosophila.Development (Cambridge, England) · 2025Article
- Non-synonymous variation and protein structure of candidate genes associated with selection in farm and wild populations of turbot (Scophthalmus maximus).Scientific reports · 2023Article
- Eya-controlled affinity between cell lineages drives tissue self-organization during Drosophila oogenesis.Nature communications · 2022Article
- The Eyes Absent Proteins: Unusual HAD Family Tyrosine Phosphatases.International journal of molecular sciences · 2021Review
- EYES ABSENT and TIMELESS integrate photoperiodic and temperature cues to regulate seasonal physiology inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Eya phosphatase: Its unique role in cancer.The international journal of biochemistry & cell biology · 2018Review
- Article
- Antagonistic regulation of the second mitotic wave by Eyes absent-Sine oculis and Combgap coordinates proliferation and specification in theDevelopment (Cambridge, England) · 2017Article
- The retinal determination gene network: from developmental regulator to cancer therapeutic target.Oncotarget · 2016Review
- Conditional knockout of retinal determination genes in differentiating cells in Drosophila.The FEBS journal · 2016Article
- Identification of novel direct targets of Drosophila Sine oculis and Eyes absent by integration of genome-wide data sets.Developmental biology · 2016Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Eyes absent (Eya) is a highly conserved transcriptional coactivator and protein phosphatase that plays vital roles in multiple developmental processes from Drosophila to humans. Eya proteins contain a PST (Proline-Serine-Threonine)-rich transactivation domain, a threonine phosphatase motif (TPM), and a tyrosine protein phosphatase domain. Using a genomic rescue system, we find that the PST domain is essential for Eya activity and Dac expression, and the TPM is required for full Eya function. We also find that the threonine phosphatase activity plays only a minor role during Drosophila eye development and the primary function of the PST and TPM domains is transactivation that can be largely substituted by the heterologous activation domain VP16. Along with our previous results that the tyrosine phosphatase activity of Eya is dispensable for normal Eya function in eye formation, we demonstrate that a primary function of Eya during Drosophila eye development is as a transcriptional coactivator. Moreover, the PST/TPM and the threonine phosphatase activity are not required for in vitro interaction between retinal determination factors. Finally, this work is the first report of an Eya-Ey physical interaction. These findings are particularly important because they highlight the need for an in vivo approach that accurately dissects protein function.
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