ArticleThe Journal of cell biology2019
Phosphorylation of CEP83 by TTBK2 is necessary for cilia initiation.
Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 85 citations in OpenAlex.
- Primary cilia dysfunction: A critical driver of metabolic diseases (Review).International journal of molecular medicine · 2026Review
- Primary cilium disassembly - from mechanisms to roles in physiology and disease.Journal of cell science · 2026Review
- Checkpoint kinase 2 coordinates autophagy activation and Aurora kinase A degradation to regulate primary cilia for cell invasion.Cell communication and signaling : CCS · 2026Article
- Expression and regulation of lncRNAs in the testes of Yili geese with high and low sperm motility.BMC genomics · 2026Article
- CCDC41 Drives Oocyte Meiotic Progression by Promoting Rab11a/Rab7-Positive Vesicle Fusion with Target Membranes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- In vitro approaches to study centriole and cilium function in early mouse embryogenesis.Life science alliance · 2026Article
- PIEZO1-Primary Cilia Axis Mediates Compressive Stress-Induced Growth Plate Degeneration and Ossification in Adolescent Idiopathic Scoliosis.JOR spine · 2025Article
- Primary cilia function as hubs for signal transduction.Cell & bioscience · 2025Review
- Stage-Resolved Phosphoproteomic Landscape of Mouse Spermiogenesis Reveals Key Kinase Signaling in Sperm Morphogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Phosphorylation at the Helm: Kinase-Mediated Regulation of Primary Cilia Assembly and Disassembly.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Strategies for multimodal spatiotemporal profiling of phosphorylation in cilia biology.Journal of cell science · 2025Review
- Prostaglandin E2 and Progesterone Receptor Coordinately Regulate Primary Cilia for Proper Decidualization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Identification of New Ciliary Signaling Pathways in the Brain and Insights into Neurological Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Post-Translational Modifications in Cilia and Ciliopathies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Insights into golgi apparatus and centrosome: implications for ciliogenesis.Molecular biology reports · 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
- Centrobin serves as a safeguard to guide timely centriole maturation during the cell cycle.Scientific reports · 2025Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Primary cilia are microtubule-based organelles that play important roles in development and tissue homeostasis. Tau-tubulin kinase-2 (TTBK2) is genetically linked to spinocerebellar ataxia type 11, and its kinase activity is crucial for ciliogenesis. Although it has been shown that TTBK2 is recruited to the centriole by distal appendage protein CEP164, little is known about TTBK2 substrates associated with its role in ciliogenesis. Here, we perform superresolution microscopy and discover that serum starvation results in TTBK2 redistribution from the periphery toward the root of distal appendages. Our biochemical analyses uncover CEP83 as a bona fide TTBK2 substrate with four phosphorylation sites characterized. We also demonstrate that CEP164-dependent TTBK2 recruitment to distal appendages is required for subsequent CEP83 phosphorylation. Specifically, TTBK2-dependent CEP83 phosphorylation is important for early ciliogenesis steps, including ciliary vesicle docking and CP110 removal. In summary, our results reveal a molecular mechanism of kinase regulation in ciliogenesis and identify CEP83 as a key substrate of TTBK2 during cilia initiation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.