ArticleScientific reports2016
C-terminal domain of p42 Ebp1 is essential for down regulation of p85 subunit of PI3K, inhibiting tumor growth.
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 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- PA2G4 in health and disease: An underestimated multifunctional regulator.Journal of advanced research · 2025Review
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- Chaperone-assisted E3 ligase CHIP: A double agent in cancer.Genes & diseases · 2022Review
- ERBB3 binding protein 1 promotes the progression of malignant melanoma through activation of the Wnt/ β-catenin signaling pathway.Cancer cell international · 2022Article
- The roles of multifunctional protein ErbB3 binding protein 1 (EBP1) isoforms from development to disease.Experimental & molecular medicine · 2020Review
- Dysregulation of Epigenetic Control Contributes to Schizophrenia-Like Behavior in Ebp1International journal of molecular sciences · 2020Article
- Article
- Neuron-specific expression of p48 Ebp1 during murine brain development and its contribution to CNS axon regeneration.BMB reports · 2017Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
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Abstract
Potential tumor suppressor p42, ErbB3-binding protein 1 (EBP1) inhibits phosphoinositide 3-kinase (PI3K) activity reducing the p85 regulatory subunit. In this study, we demonstrated that overexpression of p42 promoted not only a reduction of wild type of p85 subunit but also oncogenic mutant forms of p85 which were identified in human cancers. Moreover, we identified the small fragment of C-terminal domain of p42 is sufficient to exhibit tumor suppressing activity of p42-WT, revealing that this small fragment (280-394) of p42 is required for the binding of both HSP70 and CHIP for a degradation of p85. Furthermore, we showed the small fragment of p42 markedly inhibited the tumor growth in mouse xenograft models of brain and breast cancer, resembling tumor suppressing activity of p42. Through identification of the smallest fragment of p42 that is responsible for its tumor suppressor activity, our findings represent a novel approach for targeted therapy of cancers that overexpress PI3K.
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