Ask about this productRelated genes to: PIAS2 antibody
- Gene:
- PIAS2 NIH gene
- Name:
- protein inhibitor of activated STAT 2
- Previous symbol:
- -
- Synonyms:
- PIASX-BETA, miz, PIASX-ALPHA, ZMIZ4, ARIP3
- Chromosome:
- 18q21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-02
- Date modifiied:
- 2017-09-04
Related products to: PIAS2 antibody
Related articles to: PIAS2 antibody
- This study aimed to investigate the impact of the RNA-binding protein eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) gene, also known as PKR, on the condition of islet beta cells. In this study, EIF2AK2 was overexpressed in INS1 cells, and transcriptome data following EIF2AK2 overexpression were obtained using RNA-seq technology. Additionally, potential target genes that bind to EIF2AK2 were identified through iRIP-seq technology. The proteins interacting with EIF2AK2 were characterized using co-immunoprecipitation (CO-IP) combined with mass spectrometry to elucidate the molecular regulatory mechanisms of EIF2AK2 in INS1 cells. RNA-seq results indicated that in INS1 cells overexpressing EIF2AK2, 1171 genes were differentially expressed, and 2161 alternative splicing events were significantly altered. iRIP-seq data demonstrated that reads from the immunoprecipitated samples were significantly enriched in the intronic and coding sequence (CDS) regions. EIF2AK2 preferentially binds to the GCGGCGG motif in RNA. Comprehensive analysis suggests that EIF2AK2 may directly bind to and regulate the expression of Dusp8, Btg1, and Prkce, thereby affecting pancreatic islet cell functions. Furthermore, EIF2AK2 may influence islet cell function by modulating the alternative splicing of Zfr and Pias2. Additionally, combined with Co-IP mass spectrometry data, it was discovered that EIF2AK2 can interact with 649 proteins, including various differentially expressed RNA-binding proteins, transcription factors, and histones, which may be associated with diabetes. Our results indicate that EIF2AK2 may regulate the expression or alternative splicing of mRNA related to type 2 diabetes through direct or indirect binding. Additionally, it may influence the progression of type 2 diabetes by interacting with other proteins. We propose that EIF2AK2 plays a significant role in diabetic islet beta cells, and its aberrant regulatory pattern is closely associated with the onset and progression of type 2 diabetes. - Source: PubMed
Ning LiliLiu TongLv YuanyuanCheng YanYang MaoguangCai Hanqing - The health of pancreatic β cells is known to be under the tight control of several genetic processes, including insulin signaling, regeneration (, , , ), and calcium signaling (, , ). These signaling cascades regulate β-cell proliferation, differentiation, and insulin production and secretion and thus have been known to be the key players in diabetes pathogenesis as well as drug targets. This study aimed to elucidate the protective effect of seed extract and β-cells dietary supplement. - Source: PubMed
Publication date: 2026/01/12
Sarfraz ZahidRehman RabiaSaleem MakkiaT Al-Thagafi ZahrahA Habib MohamedB M Ibrahim AhmedAkram Mehwish - Avian influenza virus (AIV) is a significant zoonotic pathogen that causes infectious disease in various species and poses a serious threat to both the poultry industry and public health. Mammalian protein inhibitors of activated STAT2 (PIAS2) have been shown to affect viral replication by interacting with viral proteins. However, the role of chicken PIAS2 (chPIAS2) in regulating H6N2 subtype AIV replication remains unclear. In this study, we cloned chPIAS2 from primary chicken embryo fibroblast cells and identified that it contains five conserved domains. Overexpression of chPIAS2 promoted the replication of H6N2 AIV, although chPIAS2 expression was also induced during viral infection. We further found that chPIAS2 interacted with the H6N2 AIV nucleoprotein (NP) (DK65-NP) in the nucleus. ChPIAS2 promoted the SUMOylation of DK65-NP through its SUMO E3 ligase activity. We also confirmed that the lysine residues at positions 7, 48, 77, and 113 are the small ubiquitin-like modifier (SUMO) conjugation (SUMOylation) sites of DK65-NP. Collectively, our results indicate that chPIAS2 promotes H6N2 AIV replication by enhancing the SUMOylation of viral NP. In conclusion, our study reveals the role of chPIAS2 in AIV replication and provides new insights into the molecular mechanisms underlying AIV pathogenicity in poultry, suggesting a potential therapeutic target for avian influenza. - Source: PubMed
Publication date: 2025/12/18
Zhang JunshengXue QianWang XiyiYang HuixingHuang MinfanZhang MengZhao LuxiangWang WenqingChen ZuxianJiao Peirong - Head and neck squamous cell carcinoma (HNSC) stand as one of the most fatal malignancies worldwide. The intricate nature of this disease has contributed to a limited understanding of its diagnostic and prognostic indicators. This study comprehensively investigated the dysregulation of PIAS family genes (PIAS1, PIAS2, PIAS3, and PIAS4) in Head and Neck Squamous Cell Carcinoma (HNSC). - Source: PubMed
Publication date: 2025/11/20
Hussain MumtazIshfaq MehreenHameed Syeda AmberAbbas Afshan SyedBhanbhro Mujeeb Ur RehmanAin Qurat UlAbdel-Maksoud Mostafa AAlamri AbdulazizAlmutairi SaeedahAlmanaa Taghreed NAyaz Muhammad MazharHameed Yasir Introduction: Diabetic nephropathy (DN) is a common complication in diabetic patients, and the pathological mechanism has not been fully understood. PIAS2, as a counter-regulator of the JAK2/STAT3 signaling pathway, may play a crucial role in DN. This study aimed to investigate the expression of PIAS2 in high glucose-induced podocytes and the protective effect against podocyte cell injury. - Source: PubMed
Publication date: 2025/11/10
Li XiaZhang Yanxia