ArticleJournal of molecular cell biology2021
SUMOylation of α-tubulin is a novel modification regulating microtubule dynamics.
Article in Journal of molecular cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Tubulin glutamylation: a key regulator of flagella, cilia, centrosomes, and disease pathways.Journal of biomedical science · 2026Review
- TUBA8 promotes neuronal dendrite development through its 40th alanine.Journal of molecular cell biology · 2026Article
- Emerging Roles of Tubulin Isoforms and Their Post-Translational Modifications in Microtubule-Based Transport and Cellular Functions.Biomolecules · 2026Review
- KDM4A serves as an α-tubulin demethylase regulating microtubule polymerization and cell mitosis.Science advances · 2025Article
- Co-opted SUMO machinery promotes condensate formation associated with membranous replication organelles of a positive-strand RNA virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Acetylation of α-tubulin restores endothelial cell injury and blood-brain barrier disruption after intracerebral hemorrhage in mice.Experimental & molecular medicine · 2025Article
- Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap.Nature communications · 2025Article
- Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025Review
- Examination of the enrichment of neuronal extracellular vesicles from cell conditioned media and human plasma using an anti-NCAM immunocapture bead approach.BMC methods · 2025Article
- Sumo-regulatory SENP2 controls the homeostatic squamous mitosis-differentiation checkpoint.Cell death & disease · 2024Article
- Review
- SifA SUMOylation governs Salmonella Typhimurium intracellular survival via modulation of lysosomal function.PLoS pathogens · 2023Article
- Tubulin Cytoskeleton in Neurodegenerative Diseases-not Only Primary Tubulinopathies.Cellular and molecular neurobiology · 2023Review
- Deciphering the Tubulin Language: Molecular Determinants and Readout Mechanisms of the Tubulin Code in Neurons.International journal of molecular sciences · 2023Review
- Proteomic Identification of an Endogenous Synaptic SUMOylome in the Developing Rat Brain.Frontiers in molecular neuroscience · 2021Article
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Authors and funding
9 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules (MTs) are regulated by a number of known posttranslational modifications (PTMs) on α/β-tubulin to fulfill diverse cellular functions. Here, we showed that SUMOylation is a novel PTM on α-tubulin in vivo and in vitro. The SUMOylation on α-tubulin mainly occurred at Lys 96 (K96), K166, and K304 of soluble α-tubulin and could be removed by small ubiquitin-related modifier (SUMO)-specific peptidase 1. In vitro experiments showed that tubulin SUMOylation could reduce interprotofilament interaction, promote MT catastrophe, and impede MT polymerization. In cells, mutation of the SUMOylation sites on α-tubulin reduced catastrophe frequency and increased the proportion of polymerized α-tubulin, while upregulation of SUMOylation with fusion of SUMO1 reduced α-tubulin assembly into MTs. Additionally, overexpression of SUMOylation-deficient α-tubulin attenuated the neurite extension in Neuro-2a cells. Thus, SUMOylation on α-tubulin represents a new player in the regulation of MT properties.
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