Ask about this productRelated genes to: PPP2R1A antibody
- Gene:
- PPP2R1A NIH gene
- Name:
- protein phosphatase 2 scaffold subunit Aalpha
- Previous symbol:
- -
- Synonyms:
- PR65A, PP2A-Aalpha, PP2AA
- Chromosome:
- 19q13.41
- Locus Type:
- gene with protein product
- Date approved:
- 1993-01-25
- Date modifiied:
- 2018-07-18
Related products to: PPP2R1A antibody
Related articles to: PPP2R1A antibody
- Myocardial fibrosis, characterized by excessive collagen deposition and fibroblast activation, is a pivotal pathological process driving heart failure after myocardial infarction (MI). Our prior research revealed that Brahma-related gene 1 (BRG1) expression is elevated after MI and exacerbated cardiac electrophysiological remodeling; however, its precise role and molecular mechanism in post-MI fibrosis remain undefined. - Source: PubMed
Publication date: 2026/03/16
Cui YunfengJin JingCui YingtaoMa ZiyueTong TingtingXiong LisiShen MeimeiZhao YuGuo XinLiang WenZhao HongxiaBan TaoHuo Rong - Recent studies have indicated that phosphoethanolamine cytidylyltransferase 2 (PCYT2) is aberrantly expressed in various tumors, influencing tumor progression, metastasis, and drug resistance. However, the role of PCYT2 in clear cell renal cell carcinoma (ccRCC) remains unexplored. The objective of this research is to explore the expression changes of PCYT2 in ccRCC and elucidate its potential regulatory effects on ccRCC biological functions, alongside the underlying molecular mechanisms. Through sequencing data analysis and clinical tissue assessments, we discovered a notable downregulation of PCYT2 in ccRCC tissues, with lower PCYT2 expression correlating with poorer patient prognosis. Gene overexpression and silencing experiments demonstrated that PCYT2 overexpression exerted notable anti-cancer effects, including inhibition of cell proliferation, migration, and invasion. Silencing PCYT2 produced opposite effects, which could be reversed by PCYT2 overexpression. Mechanistic studies revealed that PCYT2 promoted the phosphorylation of Yes-associated protein 1 (YAP1), preventing its nuclear translocation and thereby inhibiting YAP1 pathway activation. Further investigations indicated that the regulatory effect of PCYT2 on YAP1 phosphorylation was dependent on PPP2R1A. In vivo studies corroborated these findings, showing that PCYT2 overexpression significantly restrained tumor formation, accompanied by downregulation of the YAP1 pathway. Our findings offer substantial evidence that PCYT2 acts as a tumor suppressor in ccRCC, with its mechanism linked to the regulation of YAP1 pathway activation. This study offers fresh perspectives on the molecular pathogenesis of ccRCC and identifies PCYT2 as a potential candidate for therapeutic strategies in this disease. - Source: PubMed
Publication date: 2026/03/07
Nan NingGuo HaoHuang YanChen JuanQiang Xiaolong - Pseudolarolide B (PB), a spirocyclic triterpenoid lactone derived from Pseudolarix amabilis (Nelson) Rehder, demonstrates significant anti-inflammatory properties. However, the precise molecular mechanism underlying this activity has remained elusive. Here, using activity-based protein profiling (ABPP), we identified the scaffolding subunit A (PPP2R1A) of protein phosphatase 2 A (PP2A) as the direct covalent target of PB. We further elucidated that PB covalently binds to Cys317 of PPP2R1A. This modification enhances the structural stability of the A subunit and promotes its capacity to recruit both the catalytic (C) and regulatory (B) subunits, thereby facilitating the assembly of the active PP2A holoenzyme and augmenting its phosphatase activity. Consequently, the enhanced PP2A activity led to the dephosphorylation of key proteins in critical inflammatory signaling pathways. Molecular dynamics simulations provided structural insights, confirming that PB-induced covalent modification stabilizes PPP2R1A and strengthens its interaction with the catalytic subunit. Collectively, our study delineates a novel mechanism whereby PB exerts its anti-inflammatory effects by allosterically promoting PP2A holoenzyme assembly and activity through targeting its scaffolding subunit, offering a new strategy for the pharmacological modulation of PP2 A. - Source: PubMed
Publication date: 2026/03/02
Li YutongHuang YanWang ShangyiXia HuiminLi JiangWu XianfuLu YongMa BoSu GuozhuLi Yong - Idiopathic pulmonary fibrosis (IPF) is driven by the transdifferentiation of pulmonary fibroblasts into myofibroblasts, a pivotal step in disease progression. This study aimed to determine whether platycodin D (PD), a natural compound used in traditional Chinese medicine, can inhibit this process. The findings revealed that PD alleviates lung injury, reduces inflammation and oxidative stress, and markedly suppresses myofibroblast generation in both in vivo and in vitro models. - Source: PubMed
Publication date: 2026/02/21
Gong Jia-NingCui ZanLiu Yuan-YuanMeng Ling-QiWang YiShi JiaQin Zhi-YongChen GuangChang An - To investigate the expression of tumor necrosis factor-alpha (TNF-α)-regulated circular RNAs (circRNAs) in T cells from patients with rheumatoid arthritis (RA). - Source: PubMed
Publication date: 2026/02/11
Yu Hui-ChunChen Pin-ChenHuang Hsien-BinLu Ming-Chi