PIAS4 antibody - N-terminal region (ARP33011_P050)
- Known as:
- PIAS4 (anti-) - N-terminal region (ARP33011_P050)
- Catalog number:
- arp33011_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- PIAS4 antibody - N-terminal region (ARP33011_P050)
Related genes to: PIAS4 antibody - N-terminal region (ARP33011_P050)
- Gene:
- PIAS4 NIH gene
- Name:
- protein inhibitor of activated STAT 4
- Previous symbol:
- -
- Synonyms:
- Piasg, PIASY, FLJ12419, ZMIZ6
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-02
- Date modifiied:
- 2015-11-13
Related products to: PIAS4 antibody - N-terminal region (ARP33011_P050)
Related articles to: PIAS4 antibody - N-terminal region (ARP33011_P050)
- Protein post-translational modifications are crucial in driving cancer development and progression. The SUMO E3 ligase PIAS4 regulates various cellular processes, thereby promoting tumour advancement. However, the role of PIAS4 in breast cancer remains unclear. This study aimed to examine the protein levels of PIAS4 in clinical specimens, explore PIAS4 regulates cell cycle mechanism and investigate the synergistic inhibitory effects of PIAS4 and CDK6 inhibition on breast cancer progression. Our findings revealed that PIAS4 was highly expressed in breast cancer and negatively correlated with prognosis. Abrogation of PIAS4 inhibited breast cancer cell proliferation and induced G1 phase cell cycle delay. The primary mechanism involved PIAS4-mediated SUMOylation of CDK6, which enhanced retinoblastoma 1 (RB1) phosphorylation and the transcription of downstream cell cycle genes, facilitating cell cycle G1 phase progression. We found that CDK6 underwent SUMO1 and SUMO2/3 modifications and identified the main SUMO2/3 modification sites. Mutations at these sites inhibit CDK6-mediated RB1 phosphorylation, consequently blocking cell cycle progression in the G1 phase. CDK6 kinase activity is reduced following PIAS4 knockdown, which may be associated with decreased binding of Cyclin D1 to CDK6. Moreover, in mouse xenograft models, combining PIAS4 and CDK6 inhibition enhanced therapeutic efficacy against breast cancer. Therefore, targeting PIAS4 to impede cell cycle progression may be a novel strategy for breast cancer treatment. - Source: PubMed
Publication date: 2026/04/07
Chen HuiHu XinyangFeng LifengCheng XiaoqingZhu LiyuanXu FeiZhu TaoGao YongmeiWang JinJin HongchuanJiang Zhinong - Diabetic cardiomyopathy (DCM) is characterized by metabolic dysregulation and progressive cardiac dysfunction, but the underlying molecular mechanisms remain incompletely understood. Emerging evidence suggests that 3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2) may play an important role in DCM pathogenesis. This study reveals a novel regulatory mechanism involving SIRT5-mediated post-translational modification of HMGCS2 in DCM pathogenesis using high glucose-treated cardiomyocyte models and DCM mouse models. In DCM models, HMGCS2 was significantly upregulated and found to promote cardiomyocyte pyroptosis, cardiac dysfunction, and myocardial tissue damage. In contrast, SIRT5 exhibited cardioprotective effects under the same conditions. Moreover, SIRT5 overexpression reduced HMGCS2 succinylation while enhancing its ubiquitination and degradation in cardiomyocytes under high glucose conditions. Mechanistically, SIRT5 facilitated ubiquitin-mediated degradation of HMGCS2 at K118 by upregulating the E3 ubiquitin ligase PIAS4. In conclusion, SIRT5 mediated HMGCS2 desuccinylation while promoting PIAS4-dependent HMGCS2 ubiquitination and degradation. This study identified the SIRT5/PIAS4/HMGCS2 axis as a critical regulatory pathway in DCM, suggesting that targeting SIRT5 to influence HMGCS2 post-translational modifications might offer a novel therapeutic approach for DCM. - Source: PubMed
Huang ChahuaXiong WenqiXu Yingying - Breast cancer is a significant global health issue, with resistance to doxorubicin (DOX) posing a major challenge to effective treatment. SUMOylation, a post-translational modification process, is linked to cancer progression and therapy resistance. PIAS4, a SUMO E3 ligase involved in maintaining genome stability and stress response, may play a role in these mechanisms. However, its function in breast cancer progression and DOX resistance remains uncertain. This study investigates the potential role of PIAS4 in mediating DOX resistance in breast cancer. - Source: PubMed
Publication date: 2026/01/30
Salih Mohammed A MSalem Mohamed M A E LShahid Muhammad AliElrewey Hussein A SWilliamson RitchieKantamneni Sriharsha - Irisin, a cleavage peptide by fibronectin type III domain-containing protein 5 (FNDC5), has been recognized as a promotor of osteogenesis to alleviate osteoporosis (OP). However, the detailed regulatory mechanism of osteogenesis remains unclear. This study uncovered the mechanisms underlying bone formation. - Source: PubMed
Publication date: 2026/01/20
Zou MingxiangChen WenkangLuo BangminZhang HaoweiLiu AnsongLiu JianhuaWang ChenggongZhong DaYin Ke - The use of biomimetic nanoparticles (NPs) with virus-like morphology have recently attracted research interest as novel delivery platforms and immune adjuvants. However, the exact interactions between the nanoparticles and immune cells as well as the mechanism involved are not known in detail. This motivated us to develop virus-like mesoporous silica nanoparticles (VLP) to characterize their physicochemical properties, and to determine the immune pathways induced by the particles in mouse macrophages. The results showed inclusion of spikes mimicking viral structures on the surface increased cellular uptake and enhanced immune response as compared to spherical NPs. Proteomic analysis revealed that the pathways of RIG-I-like receptor signaling, MAPK, NF-κB, and Toll-like receptor signaling were involved in regulating the immune response when macrophages interacted with VLP. When the spikes increased from 5 to 30 nm, the expression of immune-related proteins including TRAF6 and PIAS4 proteins was upregulated. This study revealed the interaction pathways and key proteins in the activation of immune response with VLP, which may provide insights to develop novel immunotherapy for enhanced efficacy. - Source: PubMed
Publication date: 2025/12/02
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