ArticleThe Journal of biological chemistry2012
Design and characterization of modular scaffolds for tubulin assembly.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.PNAS nexus · 2024Article
- Bending-torsional elasticity and energetics of the plus-end microtubule tip.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- 3D-QSAR-Based Pharmacophore Modeling, Virtual Screening, and Molecular Docking Studies for Identification of Tubulin Inhibitors with Potential Anticancer Activity.BioMed research international · 2021Article
- Design, synthesis, and biological evaluation of novel 5,6,7-trimethoxy quinolines as potential anticancer agents and tubulin polymerization inhibitors.Iranian journal of basic medical sciences · 2020Article
- Tubulin-Dependent Transport of Connexin-36 Potentiates the Size and Strength of Electrical Synapses.Cells · 2019Article
- Insight into microtubule nucleation from tubulin-capping proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Selection and Characterization of Artificial Proteins Targeting the Tubulin α Subunit.Structure (London, England : 1993) · 2019Article
- Destabilizing an interacting motif strengthens the association of a designed ankyrin repeat protein with tubulin.Scientific reports · 2016Article
- NMR Meets Tau: Insights into Its Function and Pathology.Biomolecules · 2016Review
- Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.The Journal of biological chemistry · 2014Article
- Design, construction, and characterization of a second-generation DARP in library with reduced hydrophobicity.Protein science : a publication of the Protein Society · 2013Article
- A molecular motor finds its track.Nature structural & molecular biology · 2013Article
- Structure of a kinesin-tubulin complex and implications for kinesin motility.Nature structural & molecular biology · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In cells, microtubule dynamics is regulated by stabilizing and destabilizing factors. Whereas proteins in both categories have been identified, their mechanism of action is rarely understood at the molecular level. This is due in part to the difficulties faced in structural approaches to obtain atomic models when tubulin is involved. Here, we design and characterize new stathmin-like domain (SLD) proteins that sequester tubulins in numbers different from two, the number of tubulins bound by stathmin or by the SLD of RB3, two stathmin family members that have been extensively studied. We established rules for the design of tight tubulin-SLD assemblies and applied them to complexes containing one to four tubulin heterodimers. Biochemical and structural experiments showed that the engineered SLDs behaved as expected. The new SLDs will be tools for structural studies of microtubule regulation. The larger complexes will be useful for cryo-electron microscopy, whereas crystallography or nuclear magnetic resonance will benefit from the 1:1 tubulin-SLD assembly. Finally, our results provide new insight into SLD function, suggesting that a major effect of these phosphorylatable proteins is the programmed release of sequestered tubulin for microtubule assembly at the specific cellular locations of members of the stathmin family.
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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.