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Sep 9, 2020 · These β-tubulin residues, mutated in the disease, do indeed interact with the motor domain of kinesins, as deduced from the crystal structure of kinesin-1 bound to tubulin (Cao et al., 2014; Gigant et al., 2013). β-Tubulin residues Arg262 and Asp417 make salt bridges with the kinesin residues Asp279 and Arg278, respectively, whereas β-Glu410 interacts with His156 (Figure 5 C). Therefore ...
- Marcel Knossow, Valérie Campanacci, Liza Ammar Khodja, Benoît Gigant
- 10.1016/j.isci.2020.101511
- 2020
- iScience. 2020 Sep 25; 23(9): 101511.
Jul 2, 2018 · Microtubules form from longitudinally and laterally assembling tubulin α–β dimers. The assembly induces strain in tubulin, resulting in cycles of microtubule catastrophe and regrowth. This ...
- Szymon W. Manka, Carolyn A. Moores
- 2018
Apr 19, 2018 · The transition of a GTP-tubulin dimer in solution into a GDP-tubulin dimer integrated into the microtubule lattice is a complex process that involves multiple conformational changes.
- Gary J. Brouhard, Luke M. Rice
- 2018
Sep 25, 2023 · The β-tubulin-bound GTP can be hydrolyzed upon the incorporation of the GTP-tubulin into microtubule lattice, which plays important roles in MT dynamic instability 17. When GTP-tubulin ...
May 24, 2021 · The microtubule lattice is held together by lateral and longitudinal tubulin–tubulin interactions, and these interactions are in turn regulated by the GTP hydrolysis state of the tubulin heterodimer. Furthermore, tubulin can exist in either an extended or a compacted state in the lattice.
- Joseph M. Cleary, William O. Hancock
- 2021
May 5, 2021 · To this end, we first analyzed homotypic interactions between tubulin dimers as they occur in the microtubule lattice. 19 We then inspected heterotypic interactions of tubulin and microtubules with protein partners, whose complex structures were determined to high resolution either by X-ray crystallography or by cryo-electron microscopy (http ...
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How does a microtubule lattice interact with a tubulin heterodimer?
How do microtubules interact?
What happens when a GTP-tubulin dimer is integrated into a microtubule lattice?
How do -tubulin heterodimers interact?
Do microtubules switch their lattice States in a concerted way?
How do microtubules form?
FIGURE 1 Evolution of microtubule lattice models over time. (a) A- and B-lattice models for the organization of the -tubulin heterodimer in αβ the A- and B-subfibers of the axoneme were introduced in 1974. The A-lattice was considered to be the preferred configuration for cytoplasmic microtubules. Reprinted from Figure 14 of ©1974 Amos and Klug.
