ArticleScientific reports2016
Cell surface localization of importin α1/KPNA2 affects cancer cell proliferation by regulating FGF1 signalling.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Unbiased, systematic surfaceome profiling of Acute Leukemia to identify novel immunotherapy targets.bioRxiv : the preprint server for biology · 2026Article
- NCBP1 promotes the malignant progression of Wilms' tumor through stabilization of KPNA2 mRNA.Cancer gene therapy · 2026Article
- Palmitoylated importin α recruits PKCε to the plasma membrane to drive breast cancer cell motility.bioRxiv : the preprint server for biology · 2026Article
- Highly efficient expression of DNA-peptide conjugates in growth-arrested cells.Nature communications · 2026Article
- Loss-of-Function of Two PD-Associated Proteins Confers Resistance to Rice Stripe Virus.Molecular plant pathology · 2025Article
- Oxidative stress mediates nucleocytoplasmic shuttling of KPNA2 via AKT1-CDK1 axis-regulated S62 phosphorylation.FASEB bioAdvances · 2024Article
- Extended-Synaptotagmin 1 Enhances Liver Cancer Progression Mediated by the Unconventional Secretion of Cytosolic Proteins.Molecules (Basel, Switzerland) · 2023Article
- Leakage? or Secretion? unconventional protein secretion in cancer.Oncotarget · 2023Article
- KPNA2 promotes angiogenesis by regulating STAT3 phosphorylation.Journal of translational medicine · 2022Article
- Extended-synaptotagmin 1 engages in unconventional protein secretion mediated via SEC22BProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Extracellular PKCδ signals to epidermal growth factor receptor for tumor proliferation in liver cancer cells.Cancer science · 2022Article
- Bisphenol A replacement chemicals, BPF and BPS, induce protumorigenic changes in human mammary gland organoid morphology and proteome.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Multiple subcellular localizations and functions of protein kinase Cδ in liver cancer.World journal of gastroenterology · 2022Review
- Membrane association of importin α facilitates viral entry into salivary gland cells of vector insects.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Novel insights into the interaction between long non-coding RNAs and microRNAs in glioma.Molecular and cellular biochemistry · 2021Review
- Heparan Sulfate Synthesized byMolecular cancer research : MCR · 2021Article
- Effects of Importin α1/KPNA1 deletion and adolescent social isolation stress on psychiatric disorder-associated behaviors in mice.PloS one · 2021Article
- Transportin-2 plays a critical role in nucleocytoplasmic shuttling of oestrogen receptor-α.Scientific reports · 2020Article
- Interactions of fibroblast growth factors with sulfated galactofucan from Saccharina japonica.International journal of biological macromolecules · 2020Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Importin α1 is involved in nuclear import as a receptor for proteins with a classical nuclear localization signal (cNLS). Here, we report that importin α1 is localized to the cell surface in several cancer cell lines and detected in their cultured medium. We also found that exogenously added importin α1 is associated with the cell membrane via interaction with heparan sulfate. Furthermore, we revealed that the cell surface importin α1 recognizes cNLS-containing substrates. More particularly, importin α1 bound directly to FGF1 and FGF2, secreted cNLS-containing growth factors, and addition of exogenous importin α1 enhanced the activation of ERK1/2, downstream targets of FGF1 signalling, in FGF1-stimulated cancer cells. Additionally, anti-importin α1 antibody treatment suppressed the importin α1-FGF1 complex formation and ERK1/2 activation, resulting in decreased cell growth. This study provides novel evidence that functional importin α1 is located at the cell surface, where it accelerates the proliferation of cancer cells.
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