Ask about this productRelated genes to: TNPO1 antibody
- Gene:
- TNPO1 NIH gene
- Name:
- transportin 1
- Previous symbol:
- KPNB2
- Synonyms:
- MIP, TRN, IPO2, MIP1
- Chromosome:
- 5q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-04-21
- Date modifiied:
- 2016-10-05
Related products to: TNPO1 antibody
Related articles to: TNPO1 antibody
- The sensory functions of the primary cilium require the specific enrichment of a variety of transmembrane receptors, including G-protein-coupled receptors (GPCRs). However, the molecular and cellular mechanisms governing the ciliary targeting of these receptors remain poorly understood. In our previous work, we identified Rab8 and TNPO1 as potential ciliary transport adaptors for a range of ciliary membrane proteins, including PKHD1, RP2, RDH8, ARL13B, and RHO (a GPCR), through the formation of a ternary complex with their respective ciliary targeting sequences (CTSs). In this study, we screened nine cilium-localized GPCRs and identified five that interact with both Rab8 and TNPO1 and require the two adaptors for ciliary localization. We found that ADRB2 contains two CTSs: one in the third intracellular loop and another in the C-terminal cytosolic tail. Only the C-terminal CTS interacts with Rab8 and TNPO1, and its ciliary localization is dependent on both adaptors. Our study suggests that Rab8 and TNPO1 might function as ciliary transport adaptors for a significant number of GPCRs. - Source: PubMed
Publication date: 2026/04/24
Mahajan DivyanshuMadugula ViswanadhChia Hui MinLu Lei - Nucleocytoplasmic transport relies on targeting signals within cargo polypeptides, typically as short linear motifs but sometimes as folded domains. These signals are recognized by the Karyopherin-β (Kap) family of importins, exportins, and biportins. Despite the number of Kaps, only a few linear signal classes are well-defined: the classical nuclear localization signal (cNLS) recognized by importin-α (IMPα), which in turn binds IMPβ to form the IMPα/β heterodimer, the IMPβ-binding domain, the Pro-Tyr NLS of transportin-1 (TNPO1/Kapβ2), the IK-NLS of Kap121/importin-5, and the RS/E- and RSY-NLSs of TNPO3, along with the classical nuclear export signal (NES) of exportin-1 (XPO1/CRM1) and the phosphorylated NES of yeast Msn5. This review summarizes recent structural and biochemical advances that define these signals and their recognition rules and highlights the remaining gaps in our understanding of linear signals across the Kap family. - Source: PubMed
Publication date: 2026/03/12
Wing Casey EChook Yuh Min - MAP1LC3/LC3 (microtubule associated protein 1 light chain 3) proteins have long been thought to carry out their cellular and organismal functions, including macroautophagy/autophagy, exclusively in their lipidated form, also referred to as Atg8ylation. They are anchored mainly to the phosphatidylethanolamine present in membranes through the action of two ubiquitin-like conjugation systems. Our recent work, however, uncovered a role of non-lipidated LC3s during influenza A virus (IAV) infection. We revealed that LC3s, together with the centrosomal scaffold protein PCNT (pericentrin), form a dynein adaptor complex that facilitates IAV uncoating at late endosomes (LEs). We also showed that co-opting the LC3s-PCNT complex is an alternative strategy to aggresome processing machinery (APM) hijacking via HDAC6, allowing IAV to exploit the force generated by dynein-dependent motors for virion uncoating and genome delivery in the host cytoplasm. Notably, the function of LC3s in IAV uncoating does not require their Atg8ylation or the core autophagy machinery, and PCNT's role is independent from its centrosomal localization. These findings redefine LC3s as multifunctional adaptor proteins and reveal how viruses can co-opt centrosome assembly machinery components for host invasion.: AKAP9/AKAP450- A-kinase anchoring protein 9; APM- aggresome processing machinery; IAV- influenza A virus; LC3s-I- non-lipidated LC3s; Les- late endosomes; MAP1LC3/LC3s-microtubule associated protein 1 light chain 3 proteins; MT-microtubule; NEU- neuraminidase; PCNT-pericentrin; TNPO1-transportin 1; vRNP-viral ribonucleoprotein. - Source: PubMed
Publication date: 2025/10/13
Cong YingyingReggiori Fulvio - Sphingosine and constrained analogs like FTY720 and SH-BC-893 restrain tumor growth through incompletely defined mechanisms that include protein phosphatase 2A (PP2A) activation. Here we show that these compounds directly bind not only the PP2A scaffolding subunit PPP2R1A, but also the structurally related karyopherins importin-β1 (KPNB1), transportin-1 (TNPO1), importin-5 (IPO5), and importin-7 (IPO7). Binding to sphingosine-like molecules triggers reversible unfolding of these target proteins, resulting in activation of PP2A and inhibition of importins. Although sphingosine engages these proteins, ceramide does not, suggesting that these two endogenous tumor-suppressive sphingolipids work through distinct mechanisms. Simultaneous PP2A activation and importin inhibition reduces nuclear levels of proteins that drive cancer progression and therapeutic resistance such as JUN, YAP, MYC, androgen receptor, hnRNPA1, and NF-κB under conditions where compounds that target PP2A or KPNB1 individually are inactive. These findings provide new insights into sphingolipid biology and highlight a possible path toward cancer therapeutics that could overcome drug resistance. - Source: PubMed
Publication date: 2025/06/30
Jayashankar VaishaliKubiniok PeterMcCracken Alison NGentry Rebeca GEckenstein Kazumi HSernissi LorenzoVece VitoGarsi Jean-BaptisteValles Sarah YJung SunheeHoffman Natalie CPerrochon Arielle SSelwan Elizabeth MFinicle Brendan TPitman MaryLin DaWeiBonneil ÉricXu RuijuanMao CunguiKaiser PeterFruman David AMobley DavidJang CholsoonHanessian StephenThibault PierreEdinger Aimee L - Hepatocellular carcinoma (HCC), primarily caused by chronic hepatitis B virus (HBV) infection, remains a leading cause of liver cancer worldwide. Despite advances in antiviral therapies, persistent HBV replication, mediated by covalently closed circular DNA (cccDNA), contributes to poor prognoses and frequent recurrence of HCC. This study investigates for the first time the role of circular RNA circBRWD1 in HBV-related HCC, aiming to elucidate its function and regulatory mechanism in HBV replication and hepatocarcinogenesis. Results showed that circBRWD1 was significantly overexpressed in HBV-positive HCC tissues and cell lines compared to HBV-negative controls and promoted HBV replication by increasing cccDNA accumulation. Silencing circBRWD1 markedly reduced the levels of HBV DNA, HBV surface antigen (HBsAg), HBV e antigen (HBeAg), and HBV core antigen (HBcAg), indicating its critical role in HBV replication. Functionally, circBRWD1 knockdown led to reduced cell proliferation, colony formation, and migration while increasing apoptosis in HCC cells. Mechanistic studies revealed that circBRWD1 acts as a sponge for miR-513a-5p, thereby upregulating TNPO1, a key player in promoting HCC malignancy. Rescue experiments confirmed that TNPO1 overexpression reversed the effects of circBRWD1 depletion, restoring cell proliferation, migration, and HBV replication. Additionally, circBRWD1 depletion significantly reduced tumor growth with reduced expression of TNPO1 and increased miR-513a-5p levels in a mouse xenograft model. Collectively, this study identifies circBRWD1 as a key oncogenic circRNA that facilitates HBV replication and HCC progression via the miR-513a-5p/TNPO1 axis. Targeting circBRWD1 may offer a novel therapeutic strategy for HBV-related HCC, potentially addressing the challenge of HBV persistence and improving patient outcomes. - Source: PubMed
Publication date: 2025/04/09
Geng JiabaoHuang FeiLiu QiannanWang BingjiXiong XiWang ShoumingDong YuanYu YuechengZhao Weifeng