ArticleThe Journal of biological chemistry2010
PP2A:B56{epsilon}, a substrate of caspase-3, regulates p53-dependent and p53-independent apoptosis during development.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Protein phosphatase 2A is regulated by protein kinase Cα (PKCα)-dependent phosphorylation of its targeting subunit B56α at Ser41.The Journal of biological chemistry · 2014Trial
- Combination of in vivo and in vitro phosphoproteomics determines the PP2A target repertoire on proteome scale.Cell reports methods · 2025Article
- Arabidopsis ABCG14 forms a homodimeric transporter for multiple cytokinins and mediates long-distance transport of isopentenyladenine-type cytokinins.Plant communications · 2023Article
- Protein phosphatase 2A - structure, function and role in neurodevelopmental disorders.Journal of cell science · 2021Review
- The Interaction Mechanism of Intrinsically Disordered PP2A Inhibitor Proteins ARPP-16 and ARPP-19 With PP2A.Frontiers in molecular biosciences · 2021Article
- PP2A and tumor radiotherapy.Hereditas · 2020Review
- To be or not to be: PP2A as a dual player in CNS functions, its role in neurodegeneration, and its interaction with brain insulin signaling.Cellular and molecular life sciences : CMLS · 2019Review
- Novel functions of the ubiquitin-independent proteasome system in regulatingDevelopment (Cambridge, England) · 2019Article
- Yeast Lacking the PP2A Phosphatase Regulatory Subunit Rts1 SensitizesFrontiers in genetics · 2019Article
- Transient PP2A inhibition alleviates normal tissue stem cell susceptibility to cell death during radiotherapy.Cell death & disease · 2018Article
- RNA helicase Mov10 is essential for gastrulation and central nervous system development.Developmental dynamics : an official publication of the American Association of Anatomists · 2018Article
- PP2A as the Main Node of Therapeutic Strategies and Resistance Reversal in Triple-Negative Breast Cancer.Molecules (Basel, Switzerland) · 2017Review
- The broken "Off" switch in cancer signaling: PP2A as a regulator of tumorigenesis, drug resistance, and immune surveillance.BBA clinical · 2016Review
- Members of the Rusc protein family interact with Sufu and inhibit vertebrate Hedgehog signaling.Development (Cambridge, England) · 2016Article
- Deregulation of the protein phosphatase 2A, PP2A in cancer: complexity and therapeutic options.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Review
- The effect of adenosine A1 receptor agonist and antagonist on p53 and caspase 3, 8, and 9 expression and apoptosis rate in MCF-7 breast cancer cell line.Research in pharmaceutical sciences · 2016Article
- Protein Phosphatase 2A as a Therapeutic Target in Acute Myeloid Leukemia.Frontiers in oncology · 2016Review
- Regulation of nuclear-cytoplasmic shuttling and function of Family with sequence similarity 13, member A (Fam13a), by B56-containing PP2As and Akt.Molecular biology of the cell · 2015Article
- LB100, a small molecule inhibitor of PP2A with potent chemo- and radio-sensitizing potential.Cancer biology & therapy · 2015Review
- Protein Phosphatase 2A Mediates Oxidative Stress Induced Apoptosis in Osteoblasts.Mediators of inflammation · 2015Article
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4 authors.
Funding
Abstract
Protein phosphatase 2A (PP2A) is one of the most abundantly expressed serine/threonine protein phosphatases. A large body of evidence suggests that PP2A is a tumor suppressor and plays critical roles in regulating apoptosis. PP2A is a heterotrimeric protein complex. Its substrate specificity, localization, and activity are regulated by regulatory subunits of PP2A. A recent study has demonstrated that single nucleotide polymorphism in B56ε (PPP2R5E), a B56 family regulatory subunit of PP2A, is associated with human soft tissue sarcoma. This raises the possibility that B56ε is involved in tumorigenesis and plays important roles in regulating apoptosis. However, this hypothesis has not been tested experimentally. Our previous studies revealed that B56ε regulates a number of developmental signaling pathways during early embryonic patterning. Here we report novel functions of B56ε in regulating apoptosis. We provide evidence that B56ε has both anti- and pro-apoptotic functions. B56ε suppresses p53-independent apoptosis during neural development, but triggers p53-dependent apoptosis. Mechanistically, B56ε regulates the p53-dependent apoptotic pathway solely through controlling the stability of p53 protein. In addition to its function in regulating apoptosis, we show that B56ε undergoes proteolytic cleavage. The cleavage of B56ε is mediated by caspase-3 and occurs on the carboxyl side of an evolutionarily conserved N-terminal "DKXD" motif. These results demonstrate that B56ε, a substrate of caspase-3, is an essential regulator of apoptosis. So far, we have identified an alternative translation isoform and a caspase cleavage product of B56ε. The significance of post-transcriptional regulation of B56ε is discussed.
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Registered trials
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