Mouse polyclonal to PPP2R2C, Host Mouse
- Known as:
- Mouse pab PPP2R2C, Host Mouse
- Catalog number:
- YF-PA13943
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Abfron
- Gene target:
- Mouse polyclonal PPP2R2C Host
Related genes to: Mouse polyclonal to PPP2R2C, Host Mouse
- Gene:
- PPP2R2C NIH gene
- Name:
- protein phosphatase 2 regulatory subunit Bgamma
- Previous symbol:
- -
- Synonyms:
- PR52, IMYPNO, MGC33570, PR55G, B55gamma
- Chromosome:
- 4p16.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-01-25
- Date modifiied:
- 2017-04-05
Related products to: Mouse polyclonal to PPP2R2C, Host Mouse
Related articles to: Mouse polyclonal to PPP2R2C, Host Mouse
- Radiotherapy resistance remains a major obstacle in nasopharyngeal carcinoma (NPC). This study delineates the role of protein phosphatase 2 regulatory subunit B gamma (PPP2R2C) in NPC radioresistance and its underlying mechanism to identify therapeutic targets. Through integrated bioinformatic analysis, PPP2R2C was identified as a candidate radioresistance driver. In vitro and in vivo functional assays demonstrated that PPP2R2C depletion significantly impaired NPC cell proliferation, migration, and radioresistance, while its overexpression enhanced these phenotypes. Mechanistic investigations revealed PPP2R2C inhibits radiation-induced ferroptosis, evidenced by transmission electron microscopy (TEM), lipid reactive oxygen species (ROS) quantification, malondialdehyde (MDA) assays, and immunoblotting of glutathione peroxidase 4 (GPX4) and solute carrier family 7 member 11 (SLC7A11). Crucially, immunoprecipitation-mass spectrometry (IP-MS), co-immunoprecipitation (Co-IP), and immunofluorescence (IF) confirmed PPP2R2C physically interacts with RPS27L. Further analysis via qPCR, Western blotting, cycloheximide chase, and proteasome inhibition showed PPP2R2C stabilizes RPS27L protein by blocking proteasomal degradation. RPS27L knockdown reversed PPP2R2C-mediated radioresistance and ferroptosis suppression. Clinically, high PPP2R2C expression correlated with poor patient survival. These findings establish that PPP2R2C promotes NPC radioresistance by stabilizing RPS27L to inhibit ferroptosis, positioning the PPP2R2C-RPS27L axis as a novel prognostic biomarker and therapeutic target for overcoming radioresistance. - Source: PubMed
Publication date: 2026/05/11
Fang JianboYang QiYang LuxiLiu HuiyingHu ShuluShen WeitaoZhang YuemingShen JieWei TingLyu QiongLuo PengWu XiaowenZhang JianMeng Hui - Telomeres and pericentromeres are regions of heterochromatin that are difficult to replicate. Telomeric binding factor 2 (TRF2) is a key telomere protective protein that acts against DNA damage at telomeres and allows the progression of replication forks through telomere chromatin, a region with heterochromatin features that is difficult to replicate. TRF2 is also required at pericentromeres for proper replication elongation. Here, we show that TRF2 positively regulates the activity of protein phosphatase 2A (PP2A) by activating the expression of PPP2R2C, a gene encoding an isoform of the regulatory subunit of PP2A with particularly elevated expression in neuronal tissues. Mechanistically, we provide evidence that TRF2 binds to an intronic interstitial telomeric sequence (ITS) of PPP2R2C with transactivation activity. Moreover, PPP2R2C is recruited to telomeres and pericentromeres during S phase and during replicative stress where it attenuates the DNA damage response. Finally, we show that the TRF2-dependent regulation of PPP2R2C expression plays an important role in maintaining neurodevelopment in zebrafish. These results reveal a mechanism required for normal neurodevelopment by which TRF2 attenuates DNA damage by upregulating PPP2R2C, thereby stimulating PP2A activity at two regions difficult to replicate: telomeres and pericentromeres. - Source: PubMed
Publication date: 2026/01/29
Zhai XiuyunWang CuicuiYing YilinLeong WaiianChen LianxiangWei BohuaCheng XiaojiaoHuang ShengChen QiaowenLu YimingGilson EricYe Jing - Protein phosphorylation plays a crucial role in regulating the cytoskeletal and membrane proteins at the axon initial segment (AIS). However, our knowledge of AIS-specific kinases and phosphatases is very limited. Here, we report the identification of a protein phosphatase 2A (PP2A) B55 regulatory subunit enriched at the AIS in mice: Ppp2r2c. Our results demonstrate that PP2A-B55 subunits exhibit substantial heterogeneity in their subcellular localization and function. Notably, the Ppp2r2c subunit is selectively concentrated at the AIS, and this enrichment is driven by its unique structure. Utilizing a microelectrode array system (MEA), we show that Ppp2r2c modulates neuronal activity during in vitro development. With phosphoproteomics, we further reveal that the potassium channel Kv1.2 is one of the downstream targets that link Ppp2r2c activity to neuronal excitability. Together, these data provide a critical entry point for understanding the mechanisms of PP2A-mediated local phospho-regulation at the AIS. - Source: PubMed
Publication date: 2025/12/03
Anderson Andrew PKim SanghyunMelton Allison JDing XiaoyunZhang WeiSaltzman Alexander BMalovannaya AnnaRasband Matthew NGao Yudong - Beef flavor is affected by muscle metabolites and their related regulatory genes, and the molecular regulatory mechanisms vary among different beef breeds. To provide some new ways to improve meat quality and cattle breed improvement, 24-month-old ( = 8) and yellow cattle ( = 8) were selected for comparison in this study. The result revealed that the longissimus dorsi muscle fiber diameter, protein content and a-value of were significantly higher than that of yellow cattle, but the fat content was lower than that of yellow cattle. Furthermore, meat contained notably higher levels of polyunsaturated fatty acids (PUFA) and n-3PUFA than that of yellow cattle, and also had better levels of flavor amino acids (FAAs) and sweet amino acids (SAAs), which contribute to the flavor of beef. Through comprehensive analysis of transcriptomics and metabolomics, we detected a total of 109 markedly different metabolites (DEMs) and 1,677 differentially expressed genes (DEGs) in the pectoral muscles of the two breeds. Further analysis indicated that amino acid and lipid metabolism might be the key factors contributing to the differences in meat quality and flavor between and yellow cattle, involving metabolites such as L-2-aminobutyric acid, L-glutamic acid, L-glutamine, L-serine, betaine, pantothenic acid, and taurine. Through correlation analysis, we identified genes highly associated with flavor amino acids (, ), muscle development (, , ), and lipid metabolism (, , , , , 3, , , ) related essential regulatory genes and constructed a gene-metabolite interaction network for meat quality and flavor formation in . In summary, it was shown that significant differences in muscle metabolites between and yellow cattle, especially in amino acid and lipid metabolism, may be the major reason for the differences in quality and flavor between the two types of beef. This study provides a theoretical basis for further exploring the molecular regulatory mechanisms of the differences in beef quality and flavor between and yellow cattle, and provides a reference for the development and genetic breeding of high-quality cattle breeds. - Source: PubMed
Publication date: 2025/05/14
Han LinFu RunqiFu BinlongLi QianYu YeGao HuanZhang JiaweiQi MinJin ChunjiaMao ShengyongLeng Jing - Acute myeloid leukemia (AML) is a prevalent hematologic malignancy characterized by a steady rise in morbidity and mortality rates over time. The upregulation of methyltransferase-like 14 (METTL14) expression in AML has been identified; however, its specific contributions to AML progression and underlying molecular mechanisms have yet to be elucidated. - Source: PubMed
Publication date: 2024/07/20
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