ArticleCell cycle (Georgetown, Tex.)2013
SEPT9_i1 is required for the association between HIF-1α and importin-α to promote efficient nuclear translocation.
Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- SEPT9_i1 and Septin Dynamics in Oncogenesis and Cancer Treatment.Biomolecules · 2024Review
- An oncogenic isoform of septin 9 promotes the formation of juxtanuclear invadopodia by reducing nuclear deformability.Cell reports · 2023Article
- Live-cell imaging of septins and cell polarity proteins in the growing dikaryotic vegetative hypha of the model mushroom Coprinopsis cinerea.Scientific reports · 2023Article
- Potential therapeutic effects of Ivermectin in COVID-19.Experimental biology and medicine (Maywood, N.J.) · 2022Article
- Cinnamaldehyde Downregulation of Sept9 Inhibits Glioma Progression through Suppressing Hif-1Disease markers · 2022Article
- SEPT9_i1 regulates human breast cancer cell motility through cytoskeletal and RhoA/FAK signaling pathway regulation.Cell death & disease · 2019Article
- Article
- Septin filament coalignment with microtubules depends on SEPT9_i1 and tubulin polyglutamylation, and is an early feature of acquired cell resistance to paclitaxel.Cell death & disease · 2019Article
- Regulation of mechanotransduction: Emerging roles for septins.Cytoskeleton (Hoboken, N.J.) · 2019Review
- Imaging of hypoxia-inducible factor 1α and septin 9 interaction by bimolecular fluorescence complementation in live cancer cells.Oncotarget · 2017Article
- Septins: Regulators of Protein Stability.Frontiers in cell and developmental biology · 2016Review
- Septin Mutations in Human Cancers.Frontiers in cell and developmental biology · 2016Review
- Cancer-Related Functions and Subcellular Localizations of Septins.Frontiers in cell and developmental biology · 2016Review
- Septin cooperation with tubulin polyglutamylation contributes to cancer cell adaptation to taxanes.Oncotarget · 2015Article
- Nuclear-cytoplasmatic shuttling of proteins in control of cellular oxygen sensing.Journal of molecular medicine (Berlin, Germany) · 2015Review
- Myeloid derived hypoxia inducible factor 1-alpha is required for protection against pulmonary Aspergillus fumigatus infection.PLoS pathogens · 2014Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Septin 9 isoform 1 (SEPT9_i1) protein associates with hypoxia-inducible factor (HIF)-1α to augment HIF-1 transcriptional activity. The first 25 amino acids of SEPT9_i1 (N 25) are unique compared with other members of the mammalian septin family. This N 25 domain is critical for HIF-1 activation by SEPT9_i1 but not essential for the protein-protein interaction. Here, we show that expression of N 25 induces a significant dose-dependent inhibition of HIF-1 transcriptional activity under normoxia and hypoxia without influencing cellular HIF-1α protein levels. In vivo, N 25 expression inhibits proliferation, tumor growth and angiogenesis concomitant with decreased expression levels of intratumoral HIF-1 downstream genes. Depletion of endogenous SEPT9_i1 or the exogenous expression of N 25 fragment reduces nuclear HIF-1α levels accompanied by reciprocal accumulation of HIF-1α in the cytoplasm. Mechanistically, SEPT9_i1 binds to importin-α through N 25 depending on its bipartite nuclear localization signal, to scaffold the association between HIF-1α and importin-α, which leads to facilitating HIF-1α nuclear translocation. Our data explore a new and a previously unrecognized role of a septin protein in the cytoplasmic-nuclear translocation process. This new level in the regulation of HIF-1α translocation is critical for efficient HIF-1 transcriptional activation that could be targeted for cancer therapeutics.
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