{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nODF2 was first identified as a major structural protein in the sperm tail, but subsequent work has revealed that its splice variant, commonly known as cenexin (or hCenexin1), is the predominant form found in somatic cells. Unlike the original ODF2, cenexin possesses a unique C‐terminal extension that directs its efficient localization to the mother centriole, where it plays a pivotal role in orchestrating key cell cycle events. This variant is essential for recruiting regulators such as the polo-like kinase Plk1, whose binding depends on a specific phospho‐motif, ensuring proper pericentriolar material assembly, centrosomal maturation and ultimately, bipolar spindle formation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n\nTracts of ODF2/cenexin serve as a structural scaffold at centrioles by providing docking sites for various proteins. For instance, interactions with trichoplein and taxilin family members are critical for the hierarchical assembly of subdistal appendages, ensuring proper microtubule anchorage and spindle orientation. Studies have shown that loss of ODF2 disrupts the recruitment of partners such as ninein and CEP170, leading to compromised centrosomal integrity and diminished microtubule-organizing capacity. Moreover, Cep128 has been identified as an ODF2-interacting protein, linking ODF2 to the stability of centriolar microtubules and the overall architecture of the centrosome."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "6"}]}, {"type": "t", "text": "\n\nIn addition, ODF2/cenexin interacts with other regulatory proteins such as C3G, which colocalizes with it at the mother centriole and is essential for controlling centrosome duplication and ciliary homeostasis. Disruption of these interactions leads to aberrant centriole numbers and altered primary cilium length, underscoring the importance of ODF2 in cell cycle regulation. Clinically, altered levels of ODF2 have also been associated with defects in spermatogenesis, suggesting that proper transcriptional regulation of ODF2 is critical for fertility."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Nak-Kyun Soung, Young Hwi Kang, Keetae Kim, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Pericentriolar matrix (PCM) integrity relies on cenexin and polo-like kinase (PLK)1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.E22-01-0015"}], "href": "https://doi.org/10.1091/mbc.E22-01-0015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35609215"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35609215"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Miho Ibi, Peng Zou, Akihito Inoko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Trichoplein controls microtubule anchoring at the centrosome by binding to Odf2 and ninein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.075705"}], "href": "https://doi.org/10.1242/jcs.075705"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21325031"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21325031"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Hiroka Kashihara, Shuhei Chiba, Shin-Ichiro Kanno, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cep128 associates with Odf2 to form the subdistal appendage of the centriole."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes Cells (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/gtc.12668"}], "href": "https://doi.org/10.1111/gtc.12668"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30623524"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30623524"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Dandan Ma, Fulin Wang, Rongyi Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "α-/γ-Taxilin are required for centriolar subdistal appendage assembly and microtubule organization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.73252"}], "href": "https://doi.org/10.7554/eLife.73252"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35119360"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35119360"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Sanjeev Chavan Nayak, Vegesna Radha "}, {"type": "b", "children": [{"type": "t", "text": "C3G localizes to the mother centriole in a cenexin-dependent manner and regulates centrosome duplication and primary cilium length."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.243113"}], "href": "https://doi.org/10.1242/jcs.243113"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32371504"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32371504"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Masood Abu-Halima, Anouar Belkacemi, Basim M Ayesh, et al. 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