{"id":107422,"date":"2023-04-21T16:28:54","date_gmt":"2023-04-21T20:28:54","guid":{"rendered":"https:\/\/med.virginia.edu\/cell-biology\/?p=107422"},"modified":"2026-05-22T17:01:14","modified_gmt":"2026-05-22T21:01:14","slug":"proteomic-profiling-of-the-oncogenic-septin-9-reveals-isoform-specific-interactions-in-breast-cancer-cells","status":"publish","type":"post","link":"https:\/\/med.virginia.edu\/cell-biology\/2023\/04\/21\/proteomic-profiling-of-the-oncogenic-septin-9-reveals-isoform-specific-interactions-in-breast-cancer-cells\/","title":{"rendered":"Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells"},"content":{"rendered":"<p><strong>UVA Author:<\/strong> Elias Spiliotis<br \/>\n<strong>Citation:<\/strong> Devlin L, Okletey J, Perkins G, Bowen JR, Nakos K, Montagna C, Spiliotis ET. Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells. Proteomics. 2021 Oct;21(19):e2100155. doi: 10.1002\/pmic.202100155. Epub 2021 Aug 31. PMID: 34409731; PMCID: PMC8612247.<\/p>\n<p><strong>DOI:<\/strong> <a>https:\/\/doi.org\/10.1002\/pmic.202100155<\/a><br \/>\n<strong>Pub-Med Number<\/strong>: 34409731<\/p>\n<hr \/>\n<div id=\"eng-abstract\" class=\"abstract-content selected\">\n<p>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.<\/p>\n<\/div>\n","protected":false},"excerpt":{"rendered":"<p>UVA Author: Elias Spiliotis Citation: Devlin L, Okletey J, Perkins G, Bowen JR, Nakos K, Montagna C, Spiliotis ET. Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells. Proteomics. 2021 Oct;21(19):e2100155. doi: 10.1002\/pmic.202100155. Epub 2021 Aug 31. PMID: 34409731; PMCID: PMC8612247. DOI: https:\/\/doi.org\/10.1002\/pmic.202100155 Pub-Med Number: 34409731 Septins are a family [&hellip;]<\/p>\n","protected":false},"author":1740,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"inline_featured_image":false,"footnotes":"","_links_to":"","_links_to_target":""},"categories":[13],"tags":[22],"class_list":["post-107422","post","type-post","status-publish","format-standard","hentry","category-featured-publications","tag-intranet"],"acf":false,"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.4 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells - Department of Cell Biology<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/med.virginia.edu\/cell-biology\/2023\/04\/21\/proteomic-profiling-of-the-oncogenic-septin-9-reveals-isoform-specific-interactions-in-breast-cancer-cells\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells - Department of Cell Biology\" \/>\n<meta property=\"og:description\" content=\"UVA Author: Elias Spiliotis Citation: Devlin L, Okletey J, Perkins G, Bowen JR, Nakos K, Montagna C, Spiliotis ET. Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells. Proteomics. 2021 Oct;21(19):e2100155. doi: 10.1002\/pmic.202100155. Epub 2021 Aug 31. PMID: 34409731; PMCID: PMC8612247. 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Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells. Proteomics. 2021 Oct;21(19):e2100155. doi: 10.1002\/pmic.202100155. Epub 2021 Aug 31. PMID: 34409731; PMCID: PMC8612247. 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