ArticleMolecular and cellular biology2013
The phosphatase-transcription activator EYA1 is targeted by anaphase-promoting complex/Cdh1 for degradation at M-to-G1 transition.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- The transcriptional coactivator Eya1 exerts transcriptional repressive activity by interacting with REST corepressors and REST-binding sequences to maintain nephron progenitor identity.Nucleic acids research · 2022Article
- The multi-functional eyes absent proteins.Critical reviews in biochemistry and molecular biology · 2020Review
- EYA1's Conformation Specificity in Dephosphorylating Phosphothreonine in Myc and Its Activity on Myc Stabilization in Breast Cancer.Molecular and cellular biology · 2017Article
- EYA1 expression and subcellular localization in neuroblastoma and its association with prognostic markers.Journal of cancer research & therapy · 2016Article
- Insights into APC/C: from cellular function to diseases and therapeutics.Cell division · 2016Review
- Two-way communication between the metabolic and cell cycle machineries: the molecular basis.Cell cycle (Georgetown, Tex.) · 2015Review
- Genomic organization and evolution of double minutes/homogeneously staining regions with MYC amplification in human cancer.Nucleic acids research · 2014Article
- The canonical wnt signal restricts the glycogen synthase kinase 3/fbw7-dependent ubiquitination and degradation of eya1 phosphatase.Molecular and cellular biology · 2014Article
- Functional characterization of Anaphase Promoting Complex/Cyclosome (APC/C) E3 ubiquitin ligases in tumorigenesis.Biochimica et biophysica acta · 2014Review
- CDK6 binds and promotes the degradation of the EYA2 protein.Cell cycle (Georgetown, Tex.) · 2014Article
- BOR-syndrome-associated Eya1 mutations lead to enhanced proteasomal degradation of Eya1 protein.PloS one · 2014Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The phosphatase and transactivator EYA family proteins are overexpressed in many cancer cell lines and are abundantly distributed in undifferentiated cells during development. Loss-of-function studies have shown that EYA1 is required for cell proliferation and survival during mammalian organogenesis. However, how EYA1 is regulated during development is unknown. Here, we report that EYA1 is regulated throughout the cell cycle via ubiquitin-mediated proteolysis. The level of EYA1 protein fluctuates in the cell cycle, peaking during mitosis and dropping drastically as cells exit into G(1). We found that EYA1 is efficiently degraded during mitotic exit in a Cdh1-dependent manner and that these two proteins physically interact. Overexpression of Cdh1 reduces the protein levels of ectopically expressed or endogenous EYA1, whereas depletion of Cdh1 by RNA interference stabilizes the EYA1 protein. Together, our results indicate that anaphase-promoting complex/cyclosome (APC/C)-Cdh1 specifically targets EYA1 for degradation during M-to-G(1) transition, failure of which may compromise cell proliferation and survival.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.