ArticleACS chemical biology2016
Molecular Determinants of Tubulin's C-Terminal Tail Conformational Ensemble.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- Computational perspectives on tubulin E-hook structure and mechanisms.Biophysical reports · 2026Review
- Article
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- Microtubules in Martini: Parameterizing a heterogeneous elastic-network towards a mechanically accurate microtubule.PNAS nexus · 2025Article
- Raman Spectroscopy Reveals Photobiomodulation-Induced α-Helix to β-Sheet Transition in Tubulins: Potential Implications for Alzheimer's and Other Neurodegenerative Diseases.Nanomaterials (Basel, Switzerland) · 2024Article
- Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance.Reviews on recent clinical trials · 2024Review
- TUBA4A downregulation as observed in ALSFrontiers in cellular neuroscience · 2024Article
- Glutamylation is a negative regulator of microtubule growth.Molecular biology of the cell · 2023Article
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing.Developmental cell · 2022Article
- Frontotemporal Lobar Degeneration Case with an N-TerminalBiomolecules · 2022Article
- Tracking the Amide I and αCOO- Terminal ν(C=O) Raman Bands in a Family of l-Glutamic Acid-Containing Peptide Fragments: A Raman and DFT Study.Molecules (Basel, Switzerland) · 2021Article
- α-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics.Developmental cell · 2021Article
- C-Terminal Tail Polyglycylation and Polyglutamylation Alter Microtubule Mechanical Properties.Biophysical journal · 2020Article
- The Tubulin Code in Microtubule Dynamics and Information Encoding.Developmental cell · 2020Review
- Tubulin tails and their modifications regulate protein diffusion on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy.Nature communications · 2020Article
- Microtubule glycylation promotes attachment of basal bodies to the cell cortex.Journal of cell science · 2019Article
- How cells exploit tubulin diversity to build functional cellular microtubule mosaics.Current opinion in cell biology · 2019Review
- Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
7 authors at 3 institutions in 1 country.
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Abstract
Tubulin is important for a wide variety of cellular processes including cell division, ciliogenesis, and intracellular trafficking. To perform these diverse functions, tubulin is regulated by post-translational modifications (PTM), primarily at the C-terminal tails of both the α- and β-tubulin heterodimer subunits. The tubulin C-terminal tails are disordered segments that are predicted to extend from the ordered tubulin body and may regulate both intrinsic properties of microtubules and the binding of microtubule associated proteins (MAP). It is not understood how either interactions with the ordered tubulin body or PTM affect tubulin's C-terminal tails. To probe these questions, we developed a method to isotopically label tubulin for C-terminal tail structural studies by NMR. The conformational changes of the tubulin tails as a result of both proximity to the ordered tubulin body and modification by mono- and polyglycine PTM were determined. The C-terminal tails of the tubulin dimer are fully disordered and, in contrast with prior simulation predictions, exhibit a propensity for β-sheet conformations. The C-terminal tails display significant chemical shift differences as compared to isolated peptides of the same sequence, indicating that the tubulin C-terminal tails interact with the ordered tubulin body. Although mono- and polyglycylation affect the chemical shift of adjacent residues, the conformation of the C-terminal tail appears insensitive to the length of polyglycine chains. Our studies provide important insights into how the essential disordered domains of tubulin function.
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