PIH1D1 antibody
- Known as:
- PIH1D1 (anti-)
- Catalog number:
- orb100663
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- PIH1D1 antibody
Related genes to: PIH1D1 antibody
- Gene:
- PIH1D1 NIH gene
- Name:
- PIH1 domain containing 1
- Previous symbol:
- NOP17
- Synonyms:
- FLJ20643, Pih1
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-30
- Date modifiied:
- 2018-06-05
Related products to: PIH1D1 antibody
Related articles to: PIH1D1 antibody
- The R2TP chaperone complex comprises two AAA+ proteins, RUVBL1 and RUVBL2, along with RPAP3 and PIH1D1. R2TP functions in concert with other chaperones, such as HSP90 and HSP70, to facilitate the assembly of macromolecular complexes integral to the regulation of cell growth and proliferation. Moreover, several adaptors interact with R2TP to impart substrate specificity. Nevertheless, the precise mechanism underlying R2TP-mediated complex assembly remains unknown. This review summarizes the current knowledge regarding R2TP's involvement in the assembly, stabilization, and activity of multiple protein complexes, including box C/D and H/ACA small nucleolar ribonucleoproteins (snoRNPs), spliceosome small nuclear ribonucleoproteins (snRNPs), the tuberous sclerosis complex (TSC) , axonemal dynein arms, RNA polymerases, phosphatidylinositol 3-kinase-related kinases (PIKK), and the MRE11-RAD50-NBS1 (MRN) complex. Additionally, the role of R2TP in ciliogenesis, circadian rhythm regulation, and transcriptional condensate formation is discussed. Finally, the latest structural studies pertaining to R2TP and its related complexes are examined. - Source: PubMed
Publication date: 2026/06/04
Mohamed MaryamaWu RuikaiHoury Walid A - PIWI proteins, a subfamily of the PAZ-PIWI domain (PPD) protein family, are traditionally regarded as germline factors that partner with PIWI-interacting RNAs (piRNAs) to silence transposons and regulate gene expression. However, growing evidence implicates PIWI proteins as oncogenic drivers in diverse somatic cancers, often acting through piRNA-independent mechanisms that remain incompletely understood. Here, we integrate transcriptomic, translatomic, and proteomic profiling of wild-type versus PIWIL1-knockout gastric cancer cells to uncover a non-canonical, translational role for PIWIL1, one of the four human PIWI proteins. We find that PIWIL1 selectively enhances the translation of 5'-terminal oligopyrimidine (TOP) mRNAs by activating mTOR complex 1 (mTORC1). Mechanistically, PIWIL1 interacts with the R2TP chaperone complex (RUVBL1-RUVBL2-RPAP3-PIH1D1) and promotes its association with TELO2, facilitating mTOR-RAPTOR assembly and mTORC1 activation. Functionally, PIWIL1 deficiency sensitizes gastric cancer cells to mTOR inhibition, and in clinical samples, PIWIL1 expression positively correlates with mTORC1 pathway activity. Together, these findings define a novel piRNA-independent mechanism through which PIWIL1 contributes to tumor progression, extend PIWI-mediated translational control from the germline to human cancers, and establish PIWIL1 as a potential therapeutic target for gastric cancer in synergy with mTOR inhibition. - Source: PubMed
Publication date: 2026/04/22
Fan TianquZhao JiangshaLi LingCui MeihuaZhang JiaweiChi TianShi Shuo - The functional versatility of Hsp90 relies on its association with specialized co-chaperones that regulate client recruitment and maturation. Among these, the R2TP complex, comprising RUVBL1, RUVBL2, RPAP3 (Tah1 in yeast), and PIH1D1, acts as a conserved assembly factor essential for the biogenesis of large multiprotein machineries, including RNA polymerases, snoRNPs, PIKKs, and mTOR signaling complexes. RPAP3 functions as a central scaffold within the R2TP-Hsp90 system, linking Hsp90 and Hsp70 to the RUVBL1/2 ATPase core through its TPR domains and C-terminal interaction with PIH1D1. This modular organization enables RPAP3 to integrate chaperone-mediated folding with client delivery and complex assembly. Notably, dysregulation of RPAP3 has been implicated in oncogenic processes, highlighting its biomedical relevance. This review synthesizes current structural, functional, and evolutionary insights into RPAP3, focusing on its role within the R2TP-Hsp90 machinery and its emerging connections to human disease. - Source: PubMed
Publication date: 2026/04/09
Antonio Larissa MRamos Carlos H I - - Source: PubMed
Publication date: 2026/03/16
Pemberton Chris J - Anthracyclines, key chemotherapy agents, pose cardiotoxicity risks. In a 3-year study of 89 breast cancer patients treated with doxorubicin or epirubicin, more than 50% showed reduced left ventricular ejection fraction and progressive ventricular dilation. Although troponin-I flagged acute damage, it failed to predict long-term remodeling. Using a human methylome atlas, researchers identified 33 heart-specific methylated CpG sites and validated methylated PIH1D1 (mPIH1D1) as a novel biomarker. Elevated mPIH1D1 levels strongly correlated with ventricular dilation but not left ventricular ejection fraction decline, indicating its sensitivity to early cardiac remodeling. mPIH1D1 may complement troponin-I in risk assessment and cardiotoxicity management for patients undergoing anthracycline-based chemotherapy. - Source: PubMed
Publication date: 2026/03/11
Hsu Po-YenHuang Wan-HongLee Yi-YunPassier RobertLi Szu-ChinHong Chong-LinHung Shih-KaiLin Hong-YiLin Chun-HungChien Chen-YuLi Yi-DaLee Hsiang-ChunDésaubry LaurentNebigil Canan GChan Michael W Y