Ask about this productRelated genes to: BPNT1 Blocking Peptide
- Gene:
- BPNT1 NIH gene
- Name:
- 3'(2'), 5'-bisphosphate nucleotidase 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 1q41
- Locus Type:
- gene with protein product
- Date approved:
- 1999-07-07
- Date modifiied:
- 2016-10-05
Related products to: BPNT1 Blocking Peptide
Related articles to: BPNT1 Blocking Peptide
- We identified biallelic loss-of-function BPNT1 mutations in three patients with recurrent vitamin B12-dependent megaloblastic anemia. Mechanistically, BPNT1 deficiency caused accumulation of 3'-phosphoadenosine 5'-phosphate (PAP), impaired ribosome biogenesis, and reduced ileal expression of the cubam receptor complex in Bpnt1-null mice. - Source: PubMed
Publication date: 2026/05/21
Zeng Yi-HengLi Yun-HongYuan Ru-YingZuo Dan-DanZheng Xiao-ShengXiao Wen-HaoFang Min-KunLin Bin-BinCao Chun-YanCheng Xue-WenWang NingYang TingLuo WeiChen Wan-Jin - -ε4 is the strongest common genetic risk factor for Alzheimer's disease (AD), yet many carriers remain cognitively unimpaired into late life. We tested whether a protected-ε4-first proteomic approach could identify plasma proteins associated with delayed clinical onset among ε4 carriers. - Source: PubMed
Publication date: 2026/05/01
Guen Yann LePark JunyoungPeña-Tauber AndrésGreicius Michael D - Biological sulfation reactions require 3'-phosphoadenosine-5'-phosphosulfate (PAPS) as the universal sulfate donor. While the biosynthetic pathway of PAPS has been well characterized, the phosphatase degrading PAPS remains unidentified. Here, we discover MESH1 as a PAPS phosphatase that hydrolyzes PAPS into adenosine-5'-phosphosulfate and phosphate. Our crystallographic analysis of the MESH1-PAPS complex confirms PAPS as a bona fide substrate of MESH1. We further show that MESH1 localizes to Golgi, where sulfotransferases consume PAPS to produce sulfated glycosaminoglycan (sGAG). We show that MESH1 (also known as HDDC3) knockdown enhances sGAG production in a chondrogenic cell line. Furthermore, in brachymorphic mice, Mesh1 knockout significantly elevates sGAG levels in joint cartilage and improves bone density. In Caenorhabditis elegans lacking bpnt-1, neurotoxic PAP accumulation is alleviated by MESH1 overexpression, reducing upstream PAPS levels. Our biochemical, structural and functional findings establish MESH1 as a key PAPS phosphatase and highlights its potential as a therapeutic target in disorders characterized by sulfation deficiency. - Source: PubMed
Publication date: 2026/04/10
Lin Chao-ChiehRose JoshuaZhang AlbertMirando Anthony JMestre Alexander ADing Chien-Kuang CorneliaLiao YihanChen Ssu-YuSetayeshpour YasamanWu JianliLi ZhongYan DongHilton Matthew JZhou PeiChi Jen-Tsan - Triple-negative breast cancer (TNBC) is the most aggressive subtype of breast cancer without effective targeted therapies. Integrative analysis of transcriptomic and proteomic datasets of TNBC in our center revealed that bisphosphate nucleotidase 1 (BPNT1), a member of inositol monophosphatase superfamily with poorly characterized functional and mechanistic roles in human cancer, was abnormally upregulated in TNBC and its high expression was associated with poor patient prognosis. Loss- and gain-of-function assays revealed that BPNT1 acted as a novel oncogenic driver to promote TNBC cell proliferation, migration, invasion in vitro and to accelerate xenograft tumor growth and lung metastasis in mice. Mechanistically, BPNT1 recruited E3 ubiquitin ligase STUB1 (STIP1 homology and U-box containing protein 1) to induce proteasomal degradation of tumor suppressor protein LIMA1 (LIM domain and actin binding 1), thus promoting the epithelial-mesenchymal transition process and TNBC progression. Notably, re-expression of LIMA1 in BPNT1-overexpressing cells partially attenuated BPNT1-driven EMT and malignant phenotypes of TNBC cells. Furthermore, knockdown of BPNT1 enhanced the sensitivity of TNBC cells to the chemotherapeutic agent docetaxel. Collectively, these findings uncover a previously unknown role of the BPNT1-STUB1-LIMA1 axis in progression and docetaxel resistance in TNBC, and highlight BPNT1 as a potential therapeutic target for patients with TNBC. - Source: PubMed
Publication date: 2026/01/15
Ling Yun-XiaoAndriani LisaYang Shao-YingZhao QianHuang Min-YingZhang Yin-LingZhang Fang-LinShao Zhi-MinLi Da-QiangLiu Guang-Yu - Acetylation is a conserved and pivotal RNA modification. Acetylation of tRNA occurs at C12 (acC12) in eukaryotic tRNAs. Yeast acC12 prevents tRNA from rapid tRNA decay (RTD) at higher temperatures. However, the biological function of acC12 in higher eukaryotes remains unexplored. Moreover, whether mammalian cells contain an RTD pathway is unclear. Here, we deleted Thumpd1, the indispensable factor for acC12 biogenesis, in NIH/3T3 cells. Loss of acC12 significantly reduced tRNA aminoacylation and translational efficiency physiologically, in particular, of those enriched with Ser/Leu codons with two U/A nucleotides. Remarkably, acC12 hypomodification selectively generated rapid tRNA(CAG) turnover under heat stress. We demonstrated that tRNA(CAG) was degraded by a mammalian RTD (mRTD) mechanism, consisting of Xrn1/Xrn2-mediated 5'-3' exonuclease digestion and intracellular pAp level control by Bpnt1/Bpnt2. Our results reveal both the pivotal roles of acC12 in translation and a mRTD pathway for tRNA quality control under heat stress in mammalian cells. - Source: PubMed
Publication date: 2025/07/01
Liu NaLiu BingxueMa Chun-RuiCai ZixinWang Jin-TaoChai Zi-QingZhu NanlinShao TingChen Yue-LeiLin YuWang YirongXu HongZhou Xiao-Long