ArticleProteomics2021
Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells.
Article in Proteomics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Local RhoA activation induces anillin-independent septin recruitment in interphase cells.Molecular biology of the cell · 2026Article
- The septin cytoskeleton is a regulator of intestinal epithelial barrier integrity and mucosal inflammation.JCI insight · 2025Article
- Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025Article
- Disrupting CENP-N mediated SEPT9 methylation as a strategy to inhibit aerobic glycolysis and liver metastasis in colorectal cancer.Clinical & experimental metastasis · 2024Article
- 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
- Septins as membrane influencers: direct play or in association with other cytoskeleton partners.Frontiers in cell and developmental biology · 2023Review
- Potential of blood exosomal ENAH, SEPT9, EGF, MMP-9 and CXCL8 for the early screening of breast cancer.Oncology letters · 2022Article
- ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma.Journal of cellular and molecular medicine · 2022Article
- Spatial regulation of microtubule-dependent transport by septin GTPases.Trends in cell biology · 2021Review
- The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021Review
- Article
- Simultaneous co-overexpression of Saccharomyces cerevisiae septins Cdc3 and Cdc10 drives pervasive, phospholipid-, and tag-dependent plasma membrane localization.Cytoskeleton (Hoboken, N.J.)Article
- Phosphoregulation of the septin cytoskeleton in neuronal development and disease.Cytoskeleton (Hoboken, N.J.)Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Septins are a family of multimeric GTP-binding proteins, which are abnormally expressed in cancer. Septin 9 (SEPT9) is an essential and ubiquitously expressed septin with multiple isoforms, which have differential expression patterns and effects in breast cancer cells. It is unknown, however, if SEPT9 isoforms associate with different molecular networks and functions. Here, we performed a proteomic screen in MCF-7 breast cancer cells to identify the interactome of GFP-SEPT9 isoforms 1, 4 and 5, which vary significantly in their N-terminal extensions. While all three isoforms associated with SEPT2 and SEPT7, the truncated SEPT9_i4 and SEPT9_i5 interacted with septins of the SEPT6 group more promiscuously than SEPT9_i1, which bound predominately SEPT8. Spatial mapping and functional clustering of non-septin partners showed isoform-specific differences in interactions with proteins of distinct subcellular organelles (e.g., nuclei, centrosomes, cilia) and functions such as cell signalling and ubiquitination. The interactome of the full length SEPT9_i1 was more enriched in cytoskeletal regulators, while the truncated SEPT9_i4 and SEPT9_i5 exhibited preferential and isoform-specific interactions with nuclear, signalling, and ubiquitinating proteins. These data provide evidence for isoform-specific interactions, which arise from truncations in the N-terminal extensions of SEPT9, and point to novel roles in the pathogenesis of breast cancer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.