{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ceglowski J"],"funding":["HHS | NIH | NIDDK | Division of Diabetes, Endocrinology, and Metabolic Diseases","HHS | NIH | National Institute of General Medical Sciences","NIDDK NIH HHS","Bolie Scolar Award","NIGMS NIH HHS"],"pagination":["198-227"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10883266"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(1)"],"pubmed_abstract":["The primary cilium is a critical sensory organelle that is built of axonemal microtubules ensheathed by a ciliary membrane. In polarized epithelial cells, primary cilia reside on the apical surface and must extend these microtubules directly into the extracellular space and remain a stable structure. However, the factors regulating cross-talk between ciliation and cell polarization, as well as axonemal microtubule growth and stabilization in polarized epithelia, are not fully understood. In this study, we find TTLL12, a previously uncharacterized member of the Tubulin Tyrosine Ligase-Like (TTLL) family, localizes to the base of primary cilia and is required for cilia formation in polarized renal epithelial cells. We also show that TTLL12 directly binds to the α/β-tubulin heterodimer in vit"],"journal":["EMBO reports"],"pubmed_title":["TTLL12 is required for primary ciliary axoneme formation in polarized epithelial cells."],"pmcid":["PMC10883266"],"funding_grant_id":["T32-GM136444","R01 DK064380","DK064380","T32 GM136444","R35 GM136253"],"pubmed_authors":["Neumann AJ","Hoffman HK","Ceglowski J","McCurdy BL","Moore JK","Hoff KJ","Prekeris R"],"additional_accession":[]},"is_claimable":false,"name":"TTLL12 is required for primary ciliary axoneme formation in polarized epithelial cells.","description":"The primary cilium is a critical sensory organelle that is built of axonemal microtubules ensheathed by a ciliary membrane. In polarized epithelial cells, primary cilia reside on the apical surface and must extend these microtubules directly into the extracellular space and remain a stable structure. However, the factors regulating cross-talk between ciliation and cell polarization, as well as axonemal microtubule growth and stabilization in polarized epithelia, are not fully understood. In this study, we find TTLL12, a previously uncharacterized member of the Tubulin Tyrosine Ligase-Like (TTLL) family, localizes to the base of primary cilia and is required for cilia formation in polarized renal epithelial cells. We also show that TTLL12 directly binds to the α/β-tubulin heterodimer in vit","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jan","modification":"2026-07-14T18:23:55.52Z","creation":"2025-02-19T03:51:14.807Z"},"accession":"S-EPMC10883266","cross_references":{"pubmed":["38177908"],"doi":["10.1038/s44319-023-00005-5"]}}