ArticleNature communications2024
Soluble αβ-tubulins reversibly sequester TTC5 to regulate tubulin mRNA decay.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The trial behind it
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Who cites it
11 citing papers in PubMed.
- Genome-Wide Identification and Colchicine-Responsive Expression Profiling of the Tubulins (TUA and TUB) Gene Family inBiology · 2026Article
- Integration of CCT/TRiC assembly, degradation and function: Chaperonin complexity in a cellular context.Cell stress & chaperones · 2026Review
- Tubulin autoregulation tunes microtubule dynamics to support multicellular architecture and viability.Nature communications · 2026Article
- Tubulin autoregulation mediator TTC5 regulates neuronal morphology and migration.bioRxiv : the preprint server for biology · 2026Article
- Multilayered regulation of cytoskeletal protein abundance: autoregulatory mechanisms of actin and tubulin.Experimental & molecular medicine · 2026Review
- Planarian microtubules form a network within muscle and regulate injury-induced genes essential for regeneration patterning.Development (Cambridge, England) · 2025Article
- Reversible arginine methylation of PI3KC2α controls mitotic spindle dynamics.Cell communication and signaling : CCS · 2025Article
- CARM1 regulates tubulin autoregulation through PI3KC2α R175 methylation.Cell communication and signaling : CCS · 2025Article
- Regulation of co-translational mRNA decay by PAP and DXO1 in Arabidopsis.BMC plant biology · 2025Article
- The ribosome as a platform to coordinate mRNA decay.Nucleic acids research · 2025Review
- Regulation of microtubule growth rates and their impact on chromosomal instability.Cell cycle (Georgetown, Tex.)Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Microtubules, built from heterodimers of α- and β-tubulins, control cell shape, mediate intracellular transport, and power cell division. The concentration of αβ-tubulins is tightly controlled through a posttranscriptional mechanism involving selective and regulated degradation of tubulin-encoding mRNAs. Degradation is initiated by TTC5, which recognizes tubulin-synthesizing ribosomes and recruits downstream effectors to trigger mRNA deadenylation. Here, we investigate how cells regulate TTC5 activity. Biochemical and structural proteomic approaches reveal that under normal conditions, soluble αβ-tubulins bind to and sequester TTC5, preventing it from engaging nascent tubulins at translating ribosomes. We identify the flexible C-terminal tail of TTC5 as a molecular switch, toggling between soluble αβ-tubulin-bound and nascent tubulin-bound states. Loss of sequestration by soluble αβ-tubulins constitutively activates TTC5, leading to diminished tubulin mRNA levels and compromised microtubule-dependent chromosome segregation during cell division. Our findings provide a paradigm for how cells regulate the activity of a specificity factor to adapt posttranscriptional regulation of gene expression to cellular needs.
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Registered trials
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