Ask about this productRelated genes to: PPP2CA antibody
- Gene:
- PPP2CA NIH gene
- Name:
- protein phosphatase 2 catalytic subunit alpha
- Previous symbol:
- -
- Synonyms:
- PP2Calpha, PP2AC
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-11-10
- Date modifiied:
- 2016-12-13
Related products to: PPP2CA antibody
Related articles to: PPP2CA antibody
- Mutations in Leucine-rich repeat kinase 2 (LRRK2) are the most frequent cause of late-onset familial and idiopathic Parkinson's disease (PD), known to date. Importantly, recent data from post-mortem tissue as well as biomarker studies suggest that independent of mutations, increased kinase activity of LRRK2 plays an essential role in idiopathic PD pathogenesis. Despite extensive research on LRRK2, its activation mechanism(s) and how the various mutations result in increased kinase activity and neuronal death is still not completely understood. Accumulating evidence points to LRRK2 phospho-regulation, both auto-phosphorylation and phosphorylation by other kinases, as one potential molecular trigger of its activation. LRRK2 activation and localization is regulated by phosphatases such as Protein phosphatase 1 (PP1) and Protein phosphatase 2A (PP2A), however the exact mechanism of this phospho-regulation is not known. Our data reveal that in vitro PP2A dephosphorylates sites within the RocCOR-GTPase domain of LRRK2 and as a result de-stabilizes LRRK2 dimers, with consequent reduction of its kinase activity. Strikingly, our data further highlight that LRRK2 in turn phosphorylates the catalytic subunit of the PP2A holoenzyme PPP2CA at its critical residue T304. Furthermore, LRRK2-mediated phosphorylation of PP2CA T304 alters the methylation of the C-terminus, which is crucial for both holoenzyme formation and catalytic activity. Importantly, expression of WT-PPP2CA protects from LRRK2-G2019S induced neuronal cell death, while PPP2CA-T304 mutants fail to do so, suggesting that impaired PP2A holoenzyme formation might be detrimental for LRRK2-PD. - Source: PubMed
Publication date: 2026/05/14
Athanasopoulos Panagiotis SMemou AnnaHo Franz YSoliman AhmedPots HenderikusPapadopoulou Vassilikivon Zweydorf FelixSriraman SaiganeshThouin Alexander MarcVandewynckel LaurineSibran WilliamChartier-Harlin Marie-ChristineNichols R JeremyGreggio ElisaTaymans Jean-MarcGloeckner Christian JohannesRideout Hardy JKortholt Arjan - Serine phosphorylation is an essential switch for regulating the interactions and functions of many disease-related proteins. Accordingly, stable phosphoserine mimetics constitute chemical tools to study the effects of these post-translational modifications. In this work, we present the synthesis and characterization of a novel structural analog of phosphoserine, L-3-(pentafluorophosphato-difluoromethyl)-alanine. The hyper-fluorinated amino acid was synthetically accessed in six steps starting from commercially available -Boc-L-serine methyl ester. The protected PF amino acid and peptides derived thereof were inhibitors of the protein phosphoserine phosphatase PPP2CA, demonstrating its activity as functional phosphoserine mimetic. - Source: PubMed
Publication date: 2026/05/11
Ambros Anna MagdalenaLimberg NiklasDenzinger KatrinTiemann MarkusWolber GerhardRiedel SebastianRademann Jörg - Medulloblastoma (MB) is the most common malignant pediatric brain tumor. Current therapies are associated with substantial morbidity, and prognosis remains poor in high-risk subgroups, particularly those with TP53 mutations or relapsed disease. Cellular senescence is a tumor-suppressive program implicated in MB, but its role in anti-tumor immunity remains incompletely understood. We found that protein phosphatase 2A (PP2A) regulated immunogenic senescence in MB. Genetic ablation of the PP2A catalytic subunit, PP2Ac, or depletion of the regulatory subunit PP2A-B56α induced senescence in MB models. PP2Ac-deficient senescent cells exhibited increased MHC-I expression and enhanced immunogenicity. In syngeneic orthotopic models, PP2Ac loss prolonged survival in an immune- and CD8+ T cell-dependent manner. Analysis of patient datasets showed that senescence-associated gene signatures correlated with improved survival. Single-cell transcriptomic analysis further revealed that senescent MB cells were heterogeneous and that reduced PP2A activity was associated with an immunogenic senescence state. Because the PP2A inhibitor LB-100 has limited potency and off-target effects, we developed a lipid nanoparticle platform to deliver siRNA targeting PPP2CA. LNP-siPP2Ac efficiently silenced PP2Ac in vitro and, when delivered locally in vivo, prolonged survival in a CD8+ T cell-dependent manner. Together, these findings identify PP2A as a regulator of immunogenic senescence in MB and support PP2Ac targeting as a therapeutic strategy. - Source: PubMed
Publication date: 2026/04/23
Ho Winson SMondal IshaLiu JingjingSun RaymondHuo JiaweiGao ChaoDas OishikaTieu DarenSun JingqiLin HanchenZhang PengYu JiyangLu Rongze Olivia - Persistent leukaemic stem cells (LSCs) in chronic myeloid leukaemia (CML) are insensitive to targeted tyrosine kinase inhibitors (TKIs). Identifying alternative molecular vulnerabilities may offer new therapeutic opportunities. This study aimed to identify active RAS/RAF signalling pathway components in persistent CML-LSCs using publicly available datasets to propose a novel drug combination that could synergise with TKI therapy. - Source: PubMed
Publication date: 2026/04/22
Anggriawan I Made BayuJørgensen Heather G - Apoptosis plays a significant role in osteoporosis (OP), yet a causal relationship between apoptosis gene expressions and OP remains unexplored. This study applies an integrated multi-omics analysis to establish causality between them, offering clinical treatment and prediction insights. - Source: PubMed
Publication date: 2026/03/23
Wang YixiXia LintaoXiao YangWu MingxingZhang RuiRexiti PaerhatiZhang Hui