ArticleThe Journal of biological chemistry2013
Cytosolic carboxypeptidase 5 removes α- and γ-linked glutamates from tubulin.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Tubulin glutamylation: a key regulator of flagella, cilia, centrosomes, and disease pathways.Journal of biomedical science · 2026Review
- Resilience to Diabetic Retinopathy (RDR) Is Associated with a Pre-Retinopathy Transcriptional Program Induced by Diabetes.Biomolecules · 2026Article
- Tubulin hyperglutamylation induces retinal degeneration by disrupting ciliary architecture and protein trafficking.Zoological research · 2026Article
- Tubulin monoglutamylation is sufficient to rescue the ciliary motility defects in aFrontiers in cell and developmental biology · 2026Article
- Rescue of ciliogenesis and hyperglutamylation mutant phenotype in AGBL5BMC molecular and cell biology · 2025Article
- The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylation.bioRxiv : the preprint server for biology · 2025Article
- Variants in the AGBL5 gene are responsible for autosomal recessive Retinitis pigmentosa with hearing loss.European journal of human genetics : EJHG · 2025Article
- Carboxy-terminal polyglutamylation regulates signaling and phase separation of the Dishevelled protein.The EMBO journal · 2024Article
- Article
- Review
- Genetic dissection of non-syndromic retinitis pigmentosa.Indian journal of ophthalmology · 2022Review
- Polyglutamylation: biology and analysis.Amino acids · 2022Review
- The genetic architecture of structural left-right asymmetry of the human brain.Nature human behaviour · 2021Article
- Tubulin and Tubulin Posttranslational Modifications in Alzheimer's Disease and Vascular Dementia.Frontiers in aging neuroscience · 2021Review
- The Emerging Roles of Axonemal Glutamylation in Regulation of Cilia Architecture and Functions.Frontiers in cell and developmental biology · 2021Review
- Intrinsic and Extrinsic Factors Affecting Microtubule Dynamics in Normal and Cancer Cells.Molecules (Basel, Switzerland) · 2020Review
- The combination of whole-exome sequencing and clinical analysis allows better diagnosis of rare syndromic retinal dystrophies.Acta ophthalmologica · 2019Article
- Spatiotemporal manipulation of ciliary glutamylation reveals its roles in intraciliary trafficking and Hedgehog signaling.Nature communications · 2018Article
- Tubulin Post-Translational Modifications and Microtubule Dynamics.International journal of molecular sciences · 2017Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Cytosolic carboxypeptidase 5 (CCP5) is a member of a subfamily of enzymes that cleave C-terminal and/or side chain amino acids from tubulin. CCP5 was proposed to selectively cleave the branch point of glutamylated tubulin, based on studies involving overexpression of CCP5 in cell lines and detection of tubulin forms with antisera. In the present study, we examined the activity of purified CCP5 toward synthetic peptides as well as soluble α- and β-tubulin and paclitaxel-stabilized microtubules using a combination of antisera and mass spectrometry to detect the products. Mouse CCP5 removes multiple glutamate residues and the branch point glutamate from the side chains of porcine brain α- and β-tubulin. In addition, CCP5 excised C-terminal glutamates from detyrosinated α-tubulin. The enzyme also removed multiple glutamate residues from side chains and C termini of paclitaxel-stabilized microtubules. CCP5 both shortens and removes side chain glutamates from synthetic peptides corresponding to the C-terminal region of β3-tubulin, whereas cytosolic carboxypeptidase 1 shortens the side chain without cleaving the peptides' γ-linked residues. The rate of cleavage of α linkages by CCP5 is considerably slower than that of removal of a single γ-linked glutamate residue. Collectively, our data show that CCP5 functions as a dual-functional deglutamylase cleaving both α- and γ-linked glutamate from tubulin.
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Registered trials
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.