Ask about this productRelated genes to: PINX1 Blocking Peptide
- Gene:
- PINX1 NIH gene
- Name:
- PIN2 (TERF1) interacting telomerase inhibitor 1
- Previous symbol:
- -
- Synonyms:
- PinX1, LPTL, LPTS, FLJ20565, MGC8850, Gno1, Pxr1
- Chromosome:
- 8p23.1
- Locus Type:
- gene with protein product
- Date approved:
- 2010-04-26
- Date modifiied:
- 2019-04-16
Related products to: PINX1 Blocking Peptide
Related articles to: PINX1 Blocking Peptide
- The genetic architecture of sporadic Early-Onset Alzheimer Disease (sEOAD, onset ≤65 years) remains largely unknown. To assess the de novo mutation (DNM) hypothesis, we performed a nationwide recruitment of 37 novel sEOAD patients-unaffected parents trios. After assessing known monogenic genes, we performed trio-based exome sequencing and jointly analyzed novel trios with 12 previously reported ones. Of these, we selected 16 trios for genome sequencing. We identified three patients with a pathogenic DNM in APP or PSEN1. Then, from the 46 remaining trios, we identified 38 non-synonymous coding DNM and 4 de novo copy number variants (CNVs) in exome data. Four DNM (2 novel, in SPHK2 and DDR1) and bi-allelic inherited variants in two genes affected Alzheimer disease-related genes. No significant burden of rare coding variants in exome/genome data from 5643 EOAD cases and 16097 controls was identified using nested windows centered on each DNM position, at the transcript level. From genome data, one non-coding DNM was predicted to affect splicing in an AD-associated gene, PINX1. Overall, 48% probands carried ≥1 inherited risk factor with odds ratio (OR) > 1.5 and GWAS-defined Genetic Risk Scores (GRS) distribution was more consistent with random distribution than enrichment in higher scores in probands. We confirm that DNMs in known monogenic genes explain sEOAD in a minority of cases, while candidate DNMs in other genes might account for a small proportion of additional cases. The majority of sEOAD patients may have a complex etiology including multiple inherited variants, however, GRS might not explain most of its genetic component. - Source: PubMed
Publication date: 2026/05/29
Zarea AlineCassinari KevinLecoquierre FrançoisQuenez OlivierCharbonnier CamilleSchramm CatherineLacour MorganeRousseau StéphaneRichard Anne-ClaireRovelet-Lecrux AnneLecourtois MagalieOlaso RobertBoland AnneDeleuze Jean-FrançoisGilissen ChristianVeltman Joris AVissers Lisenka ElmBellenguez CélineDols-Icardo OrioHardy JohnHolstege HenneHulsman MarcLambert Jean-CharlesMead SimonRamirez AlfredoSims Rebeccavan Swieten JohnWagner MichaelWilliams JulieBombois StéphanieBoutoleau-Bretonniere ClaireCharmard-Witkowski Ludivinede la Sayette VincentDeramecourt VincentEtcharry-Bouyx FrédériqueGabelle AudreyGueriot ClaudeLe Guyader GwenaëlLe Ber IsabelleLebouvier ThibaudMartinaud OlivierMichon AgnèsQuelin ChloéSarazin MarieSévin MathieuThauvin-Robinet ChristelWallon DavidNicolas Gaël - Chemotherapy resistance is a major factor contributing to the failure of nasopharyngeal carcinoma (NPC) treatment. Migrasomes can export damaged mitochondria out of the cell, and the timely removal of damaged mitochondria is key to cancer cell resistance. However, whether migrasomes regulate tumor resistance remains unknown. Here, we elucidated the role and mechanism of migrasomes in chemoresistance of NPC. We found that the formation of migrasomes was increased in cisplatin-resistant NPC cells, and inhibiting migrasome formation reduced cisplatin resistance. PinX1 was lowly expressed in tumor tissues of patients with high migrasome scores. Upstream mechanism analyses showed that TP53 was effectively bound to the promoter of PinX1, thereby enhancing its transcriptional activity. Knockdown of PinX1 facilitated migrasome formation via its telomerase inhibitory domain 252-328aa region binding to Rab11a, which relied on serine residues at the N-terminal 25aa site for promoting migrasome formation. Mechanistically, PinX1 recruited RanBP2 to induce the SUMOylation of Rab11a, leading to the degradation of Rab11a at the K207 site. Furthermore, PinX1 reduced cancer cell energy metabolism by inhibiting the export of damaged mitochondria via migrasomes. Collectively, TP53-activated PinX1 recruits RanBP2 to Rab11a, triggering Rab11a K207 SUMOylation and degradation, leading to impaired migrasome formation and mitochondrial transfer, and ultimately suppresses cisplatin resistance in NPC. Our study provides a new target for clinical reversal of chemotherapy resistance in patients with NPC. - Source: PubMed
Publication date: 2026/05/05
Zhang JuanWang JunqiLiang TingfengChen FangZhu ZhenchaoHe YongHu XueyongLi JingChen ShuaijunYu Chaosheng - RNA binding proteins (RBPs) are multi-faceted proteins that interact with transcripts in various RNA driven processes and functions. However, in situ covalent capture techniques for screening authentic RNA substrates of RBPs remain challenging in terms of reproducibility, specificity, and sensitivity. Here, we developed CuCLIP-seq (CuAAC-Crosslinking and Immunoprecipitation Sequencing), an alternative in situ covalent capture sequencing method which utilizes CuAAC reaction to crosslink RBP-RNA between azido groups of RBPs and ethynyl groups of RNA molecules, followed by streptavidin-mediated enrichment of RNA substrates and high-throughput sequencing. We demonstrate the reliability of CuCLIP-seq by identifying substrate RNAs of several RBPs, including PTBP1, ADAR2, SRSF2, HNRNPA1, and PINX1, especially for capturing low-abundance targets. Additionally, this approach is authenticated by specifically resolving the alternative splicing transcripts targeted by PTBP1 and RNA targets by PINX1. Thus, this technique offers a sensitive and specific approach for detecting RBP substrates with high reproducibility, potential scalability, and wide applicability. - Source: PubMed
Publication date: 2026/04/24
Wang XingWang Meng-KeYao Bo-FeiGao Chun-ChunJin Han-FeiChen Yu-ShengWu Er-ZhongLi AngHao Ya-JingZhao Yong-LiangYang Yun-GuiYang Ying - - Source: PubMed
Publication date: 2025/09/25
Qiu JiepingXia YingBao YaweiCheng JingjingLiu LeiQian Dong - The human liver-related putative tumor suppressor LPTS/PinX1 is a gene encoding a telomerase inhibitory protein. Overexpression of LPTS/PinX1 protein can inhibit the growth of multiple telomerase-positive cancer cell lines. LPTS/PinX1 has therapeutic potential for cancer. - Source: PubMed
Publication date: 2025/08/15
Zhou HongchangZhang XiaoyingWang YaoWu YongqiangWang LingHu ChenZhang TingZhang HuiYou DianZhao MengliZhao MujunLi AnqiChen Guangming