Ask about this productRelated genes to: PTPN14 antibody
- Gene:
- PTPN14 NIH gene
- Name:
- protein tyrosine phosphatase non-receptor type 14
- Previous symbol:
- -
- Synonyms:
- PEZ
- Chromosome:
- 1q32.3-q41
- Locus Type:
- gene with protein product
- Date approved:
- 1995-02-22
- Date modifiied:
- 2019-02-14
Related products to: PTPN14 antibody
Related articles to: PTPN14 antibody
- Human papillomavirus type 16 (HPV16) is the most prevalent carcinogenic HPV type. Many HPV16 sequence variants have been described, some of which cause protein-coding mutations. However, most experiments have characterized the viral proteins encoded by the HPV16 prototype clone, and some researchers have proposed that variants identified in high-grade lesions and cancers may have higher oncogenic potential than the prototype. To determine whether oncoproteins encoded by such variants have greater oncogenic potential than the prototype version, we performed a comparative biochemical analysis of selected naturally occurring HPV16 E6 and E7 variant alleles identified in cervical lesions and/or control samples. We examined interactions of prototype and HPV16 E7 variant alleles with the retinoblastoma tumor suppressor pRB, the ubiquitin ligase UBR4 (p600), and the tumor suppressor PTPN14. We also compared HPV16 E6 prototype and variant protein interactions with the p53 tumor suppressor, the UBE3A (E6AP) ubiquitin ligase, and the PDZ-domain protein SCRIB. Several E6 or E7 variant proteins exhibited reduced binding to these cellular targets, suggestive of partial or complete loss of function. Our findings reveal that protein-protein interactions that enable the oncogenic activities of HPV16 E6 and E7 can be missing from naturally occurring HPV16 variants and that bona fide loss-of-function variants can be detected in high-grade cervical lesions or cancers. We conclude that clinical association alone is insufficient to predict the pathogenic potential of HPV16 E6 or E7 variant proteins.IMPORTANCEHuman papillomavirus type 16 (HPV16) is the leading cause of HPV-associated cancers, and most functional studies have been performed with the prototype viral clone. Numerous naturally occurring HPV16 variants have been detected in cervical lesions and cancers, raising the possibility that some variants may possess enhanced transforming activity. E6 and E7 are the major oncoproteins encoded by HPV16. By comparing key molecular interactions of prototype and naturally occurring E6 and E7 variant proteins, we found that several variant proteins display reduced engagement with tumor suppressors and ubiquitin ligases that are important for oncogenic activities. Notably, some variants found in high-grade lesions and cancers show partial or complete loss of engaging these critical host proteins. These findings indicate that the presence of an HPV16 variant in a cancer does not necessarily imply increased oncogenic potency. Functional characterization is therefore essential to interpret the biological and clinical significance of HPV16 genetic diversity. - Source: PubMed
Publication date: 2026/03/30
Grace MirandaBeeravolu HarshitaAlhamshari AhmadSkelin JosipaKiessling Si-YoungBohm AndrewWhite Elizabeth AMunger Karl - High-risk human papillomavirus (HPV) E7 proteins bind and inactivate host cellular tumor suppressors and are essential for the immortalization of primary human keratinocytes. E7 proteins from high- and low-risk HPV genotypes bind directly to at least two tumor suppressors, RB1 and PTPN14, and inactivate both. We previously characterized mutations in high-risk HPV E7 proteins that selectively abrogate the ability of E7 to bind either RB1 or PTPN14. Here, we established a genetic complementation system using the E7 mutants defective for binding to RB1 or PTPN14. Neither mutant alone could extend the lifespan of primary keratinocytes. When expressed together, the mutants could, like wild-type high-risk HPV E7, extend keratinocyte lifespan. Both high- and low-risk E7 reduced PTPN14 protein levels and reduced expression of keratinocyte differentiation genes, whereas only high-risk E7 reduced steady-state RB1 levels and induced E2F-dependent genes. Depletion of either RB1 or PTPN14 could cooperate with low-risk HPV6 E7 to extend keratinocyte lifespan, prompting the observation that PTPN14 depletion and RB1 inactivation by HPV E7 acted synergistically to induce certain cell cycle regulatory genes. Our findings advance the model that inactivation of at least two tumor suppressors is required for the carcinogenic activity of high-risk HPV E7. Although RB1 and PTPN14 regulate distinct signaling pathways, their combined inactivation may also contribute to the biological activity of HPV E7. - Source: PubMed
Publication date: 2026/03/17
Ramesh Pushkal SinduvadiNicolaci Angelo AGraham Leah ENouel JoangelaXu KevinBinning Jennifer MMunger KarlWhite Elizabeth A - Although immune dysregulation is implicated in both autoimmune diseases and cancer, comparative pathogenesis and immune response mechanisms between systemic lupus erythematosus (SLE) and colorectal cancer (CRC) remain elusive. This study identifies common molecular biomarkers and pathogenic pathways shared between SLE and CRC via multi-omics analysis. - Source: PubMed
Publication date: 2026/02/26
Guan HuiTian ChengziZhong MingZhang LihuanWang WenjingHuang MingchengChen Duo - Preeclampsia (PE) is a leading cause of maternal and perinatal mortality. Placental dysfunction drives the onset of the condition through inadequate spiral artery remodeling and ischemia-hypoxia, triggering endothelial cell injury mediated by small extracellular vesicles (sEVs), which can increase long-term cardiovascular risk in both mothers and offspring. However, the mechanisms underlying this process remain unclear and unpredictable. Although placental sEVs carry dysfunctional miRNAs associated with endothelial injury, traditional methods of separation from plasma/explantations are subject to contamination and physiological irrelevance. Tissue-derived sEVs extracted by enzymatic digestion have higher fidelity but remain unexplored in the placenta and PE. PTPN14 (a tyrosine phosphatase regulating YAP1 nuclear exclusion) also inhibits endothelial function, but its role in PE remains unclear. - Source: PubMed
Publication date: 2026/02/16
Wang YixinLin QimeiLi RuiYu JingXie LuluWang ShuqiPan KaiLi YaqiCao JiasongChang YingLi Zongjin - This study aimed to investigate the impact of lenvatinib combined with vitamin K2 on hepatocellular carcinoma (HCC) cells and to explore the underlying mechanisms. - Source: PubMed
Publication date: 2026/02/06
Zhang YuliChen DingguiQian XianfengLong ChunmeiZheng Zhongwei