Ask about this productRelated genes to: PPP4C antibody
- Gene:
- PPP4C NIH gene
- Name:
- protein phosphatase 4 catalytic subunit
- Previous symbol:
- -
- Synonyms:
- PP4, PPX
- Chromosome:
- 16p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-01-22
- Date modifiied:
- 2015-11-17
Related products to: PPP4C antibody
Related articles to: PPP4C antibody
- The protein phosphatase PPP4C has been implicated in oncogenic processes, but its role in thyroid carcinoma (THCA) and triple-negative breast cancer (TNBC) remains unclear. Here, we combined bioinformatic analyses with in vitro experiments to investigate the clinical and functional significance of PPP4C in these malignancies. PPP4C was significantly upregulated in both THCA and TNBC compared with normal tissues, and higher expression was associated with adverse clinicopathological features and poorer overall survival. Functional assays showed that PPP4C knockdown suppressed proliferation, migration, and invasion in TNBC and THCA cell lines, supporting a pro-tumorigenic role in vitro. Integrative analyses further suggested that elevated PPP4C expression is associated with oncogenic signaling pathways, RNA modification-related genes, and immune-related characteristics. Drug sensitivity prediction analysis indicated differential responsiveness to selected targeted agents, and experimental validation demonstrated that PPP4C depletion enhances sensitivity to specific inhibitors in vitro. Overall, PPP4C is consistently overexpressed and functionally relevant in THCA and TNBC. PPP4C may represent a candidate biomarker associated with tumor progression and therapeutic response, warranting further mechanistic and in vivo investigation. - Source: PubMed
Publication date: 2026/05/04
Li HuashuiChen YifanGuo GuodongLuo QinghuaLin QiangXie WenjunYan Maolin - - Source: PubMed
Publication date: 2026/04/09
Zhang LiliChen DengwangLi MingzhenLi XiaoyuWang YingPei Xiaojuan - Abnormal expression of mammalian sterile 20-like kinase 4 (MST4) has been frequently linked to cancer development. This study explores the function of MST4 in non-small cell lung cancer (NSCLC) and delves into its functional mechanism. The expression and clinical indicative values of MST4 in NSCLC were analyzed using tissue microarrays. Gain- and loss-of-function experiments of MST4 were conducted in NSCLC cell lines to identify its effects on cell growth in vitro. Transfected NSCLC cells were co-cultured with natural killer (NK) cells to analyze immune resistance. Mouse NSCLC cells 3LL were transplanted into C57BL/6 mice to generate subcutaneous or orthotopic isograft tumor models. Upstream and downstream factors of MST4 were identified using bioinformatics. MST4 was under-expressed in NSCLC tissue microarrays and human NSCLC cells. MST4 overexpression suppressed growth activity of NSCLC cells in vitro, reduced expression of immune checkpoint genes, and reduced cell resistance to NK cell cytotoxicity. Reverse trends were observed in MST4-silenced cells. In vivo, MST4 overexpression inhibited tumorigenic activity of 3LL cells in mice and reduced immunosuppressive factors in tumor tissues. Regarding the mechanism, MST4 induced phosphorylation and cytoplasmic degradation of YAP1 by influencing the MAP4K2-LATS1/2 cascade. Protein phosphatase 4 catalytic subunit (PPP4C) was found to interact with MST4 and reduce its function, thus promoting growth and immunosuppression in NSCLC by activating YAP1. This study demonstrates that PPP4C-mediated MST4 degradation contributes to growth activity and immunosuppression in NSCLC by restoring YAP1 activity, suggesting PPP4C and MST4 as potential targets for NSCLC management. - Source: PubMed
Publication date: 2026/02/12
Xu ZhengshuiGao JianiYe ChangchunLi YuZhao DanwenLi LiangSun LiangzhangCheng YaoLi WendengJiang JiantaoLiu Shiyuan - During the first meiotic division, oocytes inevitably undergo physiological DNA double-strand breaks (DSBs), which are primarily repaired through Bloom (BLM) helicase-mediated homologous recombination repair (HRR). This study investigated the consequences of BLM helicase suppression on meiotic maturation in goat oocytes, revealing that BLM helicase exhibited nuclear-predominant expression over cytoplasmic localization during meiosis I/meiosis II stages and colocalized with spindle fibers. Functional impairment of BLM helicase blocked oocyte maturation, accompanied by dysregulated expression of cumulus expansion-related genes, downregulation of oocyte paracrine factors, elevated reactive oxygen species accumulation, compromised mitochondrial function, upregulated endoplasmic reticulum stress-responsive genes, impaired autophagolysosomal activity, and disrupted Golgi distribution and ribosome function, though mitochondrial fusion and fission remained unaffected. Transcriptomics and reverse transcription quantitative polymerase chain reaction (RT-qPCR) analysis further demonstrated that the inhibition of BLM significantly downregulated expression of HRR-associated genes (REC8, PPP4C) while upregulating non-homologous end joining-associated genes (DCLRE1B, ERCC4), suggesting that BLM helicase deficiency may shift DSB repair from HRR to error-prone non-homologous end joining. Consistently, immunofluorescence staining revealed a significant increase in the DNA damage response factor phosphorylated ATM and the repair protein RAD51, indicating that BLM inhibition induces substantial DNA damage in oocytes. These results demonstrate that BLM plays a critical role in maintaining nuclear genomic stability in oocytes. This study highlights BLM helicase as a critical regulator of organelle homeostasis during meiotic progression and provides novel mechanistic insights into its multifaceted roles in oocyte maturation. - Source: PubMed
An DongweiXu JialiChen JiaqiLi ZiyangZhou BoLiu HuanChen XiangRuan Yong - Deletion and duplication of the 16p11.2 genomic locus are associated with opposing changes in brain size. To determine cellular mechanisms that underlie these opposing phenotypes, we performed quantitative phosphoproteomic analyses of induced pluripotent stem cells (iPSCs)-derived neural progenitor cells (NPCs) obtained from unaffected individuals, 16p11.2 deletion, and 16p11.2 duplication carriers. Differentially phosphorylated proteins were enriched in centrosomal and cilia proteins. Deletion NPCs showed longer primary cilium compared to unaffected individuals, while stunted cilia were observed in duplication NPCs. Through cellular screens in NPCs, we determined the contribution of genes within the 16p11.2 locus to cilium length. Protein kinase TAOK2 and phosphatase PPP4C were found to regulate primary cilia length. NPCs lacking TAOK2 exhibited elongated cilia, aberrant IFT88 and pericentrin (PCNT) accumulation, and were impaired in sonic hedgehog (SHH) signaling. These findings implicate aberrant cilia length in the pathophysiology of 16p11.2 copy number variation and establish TAOK2 kinase as a regulator of primary cilium length. - Source: PubMed
Publication date: 2025/08/28
Byeon SujinFerreccio AmyCornell MoiraOses-Prieto Juan ADeshpande AditiManvi SiriBlencowe AlisonWeiss Lauren ABurlingame Alma LYadav Smita