ArticleeLife2015
Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 69 citations in OpenAlex.
- Mechanistic insights on spatiotemporal control of Ras-signaling.Biological chemistry · 2026Review
- A unified mechanism for tubulin cofactors catalyzing α/β-tubulin biogenesis and degradation.Science advances · 2026Article
- Cryo-EM structures of the tubulin cofactors reveal the molecular basis of alpha/beta-tubulin biogenesis.Nature communications · 2025Article
- Neuroprotective Potential of the Flavonoids Quercetin and Epicatechin in a C. elegans Tauopathy Model.Molecular nutrition & food research · 2025Article
- CEP162: A critical regulator of ciliary transition zone assembly and its implications in ciliopathies.Journal of cell communication and signaling · 2025Review
- Subcellular systems follow Onsager reciprocity.npj biomedical innovations · 2025Article
- Cryo-ET suggests tubulin chaperones form a subset of microtubule lumenal particles with a role in maintaining neuronal microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Arl2 GTPase associates with the centrosomal protein Cdk5rap2 to regulate cortical development via microtubule organization.PLoS biology · 2024Article
- A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.Molecular cell · 2023Article
- Targeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS.Signal transduction and targeted therapy · 2023Review
- Tubulin isotype regulation maintains asymmetric requirement for α-tubulin over β-tubulin.The Journal of cell biology · 2023Article
- The baseless mutant links protein phosphatase 2A with basal cell identity in the brown alga Ectocarpus.Development (Cambridge, England) · 2023Article
- High Expression of Microtubule-associated Protein TBCB Predicts Adverse Outcome and Immunosuppression in Acute Myeloid Leukemia.Journal of Cancer · 2023Article
- Arf-like Protein 2 (ARL2) Controls Microtubule Neogenesis during Early Postnatal Photoreceptor Development.Cells · 2022Article
- Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT.Cell · 2022Article
- ERK1/2 Signalling Pathway Regulates Tubulin-Binding Cofactor B Expression and Affects Astrocyte Process Formation after Acute Foetal Alcohol Exposure.Brain sciences · 2022Article
- STRIPAK regulation of katanin microtubule severing in the Caenorhabditis elegans embryo.Genetics · 2022Article
- Acetylated α-tubulin K394 regulates microtubule stability to shape the growth of axon terminals.Current biology : CB · 2022Article
- Decreased tubulin-binding cofactor B was involved in the formation disorder of nascent astrocyte processes by regulating microtubule plus-end growth through binding with end-binding proteins 1 and 3 after chronic alcohol exposure.Frontiers in cellular neuroscience · 2022Article
- Target-Sequencing of Female Infertility Pathogenic Gene Panel and a Novel TUBB8 Loss-of-Function Mutation.Frontiers in genetics · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Microtubule dynamics and polarity stem from the polymerization of αβ-tubulin heterodimers. Five conserved tubulin cofactors/chaperones and the Arl2 GTPase regulate α- and β-tubulin assembly into heterodimers and maintain the soluble tubulin pool in the cytoplasm, but their physical mechanisms are unknown. Here, we reconstitute a core tubulin chaperone consisting of tubulin cofactors TBCD, TBCE, and Arl2, and reveal a cage-like structure for regulating αβ-tubulin. Biochemical assays and electron microscopy structures of multiple intermediates show the sequential binding of αβ-tubulin dimer followed by tubulin cofactor TBCC onto this chaperone, forming a ternary complex in which Arl2 GTP hydrolysis is activated to alter αβ-tubulin conformation. A GTP-state locked Arl2 mutant inhibits ternary complex dissociation in vitro and causes severe defects in microtubule dynamics in vivo. Our studies suggest a revised paradigm for tubulin cofactors and Arl2 functions as a catalytic chaperone that regulates soluble αβ-tubulin assembly and maintenance to support microtubule dynamics.
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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.