ArticleMolecular biology of the cell2020
Phosphorylation of multiple proteins involved in ciliogenesis by Tau Tubulin kinase 2.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 46 citations in OpenAlex.
- Primary cilium disassembly - from mechanisms to roles in physiology and disease.Journal of cell science · 2026Review
- Development of Potent and Cell Active 5-Azaindole-Based Tau Tubulin Kinase Inhibitors.bioRxiv : the preprint server for biology · 2026Article
- TTBK2-Driven Ciliogenesis Is Required for Intrinsic Neuronal Regeneration After Spinal Cord Injury.CNS neuroscience & therapeutics · 2026Article
- Intraflagellar transport-associated CCDC92 is required for spermiogenesis and male fertility in mice.Journal of molecular cell biology · 2025Article
- Phosphorylation at the Helm: Kinase-Mediated Regulation of Primary Cilia Assembly and Disassembly.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Stage-Resolved Phosphoproteomic Landscape of Mouse Spermiogenesis Reveals Key Kinase Signaling in Sperm Morphogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Strategies for multimodal spatiotemporal profiling of phosphorylation in cilia biology.Journal of cell science · 2025Review
- TTBK2 affects sperm quality by regulating the expression of centrosomal proteins and flagellar transporters during spermiogenesis in mice.Molecular human reproduction · 2025Article
- Coordinated roles of the CEP164 homodimer and TTBK2 are required for recruitment of the IFT machinery to the mother centriole for ciliogenesis.Molecular biology of the cell · 2025Article
- Cilia at the crossroad: convergence of regulatory mechanisms to govern cilia dynamics during cell signaling and the cell cycle.Cell & bioscience · 2025Review
- Mutually independent and cilia-independent assembly of IFT-A and IFT-B complexes at mother centriole.Molecular biology of the cell · 2025Article
- Tau-tubulin kinase 2 restrains microtubule-depolymerizer KIF2A to support primary cilia growth.Cell communication and signaling : CCS · 2025Article
- A hierarchical pathway for assembly of the distal appendages that organize primary cilia.eLife · 2025Article
- Myristoylated Neuronal Calcium Sensor-1 captures the preciliary vesicle at distal appendages.eLife · 2025Article
- CCDC92 promotes podocyte injury by regulating PA28α/ABCA1/cholesterol efflux axis in type 2 diabetic mice.Acta pharmacologica Sinica · 2024Article
- Spinocerebellar ataxia type 11 (SCA11): TTBK2 variants, functions and associated disease mechanisms.Cerebellum (London, England) · 2024Review
- Article
- A novel coiled-coil domain containing-related gene signature for predicting prognosis and treatment effect of breast cancer.Journal of cancer research and clinical oncology · 2023Article
- Tau tubulin kinase 1 and 2 regulate ciliogenesis and human pluripotent stem cells-derived neural rosettes.Scientific reports · 2023Article
- Modulation of tau tubulin kinases (TTBK1 and TTBK2) impacts ciliogenesis.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Primary cilia are organelles necessary for proper implementation of developmental and homeostasis processes. To initiate their assembly, coordinated actions of multiple proteins are needed. Tau tubulin kinase 2 (TTBK2) is a key player in the cilium assembly pathway, controlling the final step of cilia initiation. The function of TTBK2 in ciliogenesis is critically dependent on its kinase activity; however, the precise mechanism of TTBK2 action has so far not been fully understood due to the very limited information about its relevant substrates. In this study, we demonstrate that CEP83, CEP89, CCDC92, Rabin8, and DVL3 are substrates of TTBK2 kinase activity. Further, we characterize a set of phosphosites of those substrates and CEP164 induced by TTBK2 in vitro and in vivo. Intriguingly, we further show that identified TTBK2 phosphosites and consensus sequence delineated from those are distinct from motifs previously assigned to TTBK2. Finally, we show that TTBK2 is also required for efficient phosphorylation of many S/T sites in CEP164 and provide evidence that TTBK2-induced phosphorylations of CEP164 modulate its function, which in turn seems relevant for the process of cilia formation. In summary, our work provides important insight into the substrates-TTBK2 kinase relationship and suggests that phosphorylation of substrates on multiple sites by TTBK2 is probably involved in the control of ciliogenesis in human cells.
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