{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSEPTIN11 is a member of the conserved septin family of cytoskeletal GTPases that co‐assembles with other septins to form filamentous structures important for maintaining cellular architecture. Early studies demonstrated that SEPTIN11 is a component of septin complexes along stress fibers, interacting via its divergent terminal regions with partners such as SEPT2, SEPT7, SEPT8, and SEPT9 to form distinct filament networks (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, immunohistochemical analyses in retinal tissues have revealed robust expression of SEPTIN11 in proliferative membranes, suggesting its involvement in tissue remodeling processes (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Moreover, RNA interference experiments in HeLa cells indicate that depletion of SEPTIN11 affects cell size and notably leads to an increased susceptibility to bacterial invasion, even though overall actin integrity and SEPTIN9 localization remain unaltered (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in filament assembly, SEPTIN11 is a key regulator in host–pathogen interactions. Detailed analyses of septin–mediated pathways have shown that SEPTIN11, together with other septins, participates in modulating receptor functions—for instance, anchoring the Met receptor to the actin cytoskeleton during InlB-mediated entry of Listeria monocytogenes, thereby influencing the strength of ligand–receptor interactions at the plasma membrane (see"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "and."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Similarly, during Chlamydia trachomatis infection, SEPTIN11 integrates with SEPT2, SEPT7, and SEPT9 to form fibrillar structures that recruit and stabilize actin around the inclusions, contributing to the regulated egress of the pathogen (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its fundamental roles in structural organization and microbial defense, SEPTIN11 has been implicated in various disease contexts. Proteomic studies have identified SEPTIN11 as an enriched component of detergent-resistant aggregates in neurodegenerative disorders such as frontotemporal lobar degeneration (FTLD-U), suggesting a potential involvement in protein aggregation pathology (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " Its expression in human adipose tissue has also been characterized, raising the possibility that SEPTIN11 might influence adipocyte metabolism and related metabolic conditions (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Furthermore, recent work in hepatocellular carcinoma (HCC) models has revealed that SEPTIN11 acts as an oncogene by promoting Rho GTPase activation, leading to cytoskeletal rearrangements that enhance cell migration and invasion, thereby contributing to tumor metastasis (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Koh-ichi Nagata, Tomiko Asano, Yoshinori Nozawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M406153200"}], "href": "https://doi.org/10.1074/jbc.M406153200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15485874"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15485874"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Xiaorong Xin, Mona Pache, Barbara Zieger, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Septin expression in proliferative retinal membranes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Histochem Cytochem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1369/jhc.7A7188.2007"}], "href": "https://doi.org/10.1369/jhc.7A7188.2007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17625225"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17625225"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Serge Mostowy, Anne Danckaert, To Nam Tham, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "A role for septins in the interaction between the Listeria monocytogenes INVASION PROTEIN InlB and the Met receptor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biophys J (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bpj.2011.02.040"}], "href": "https://doi.org/10.1016/j.bpj.2011.02.040"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21504731"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21504731"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Larisa Volceanov, Katharina Herbst, Martin Biniossek, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Septins arrange F-actin-containing fibers on the Chlamydia trachomatis inclusion and are required for normal release of the inclusion by extrusion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "mBio (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/mBio.01802-14"}], "href": "https://doi.org/10.1128/mBio.01802-14"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25293760"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25293760"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Yair M Gozal, Nicholas T Seyfried, Marla Gearing, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The cytoskeletal protein septin 11 is associated with human obesity and is involved in adipocyte lipid storage and metabolism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetologia (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00125-016-4155-5"}], "href": "https://doi.org/10.1007/s00125-016-4155-5"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27866222"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27866222"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Lisheng Fu, Xiaoyan Wang, Ying Yang, et al. 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