Regulation of microtubule dynamic instability by the carboxy-terminal tail of β-tubulin
| Autor: | Colby P. Fees, Jeffrey K. Moore |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Ecology biology Chemistry Health Toxicology and Mutagenesis Cell Mutant Plant Science macromolecular substances Biochemistry Genetics and Molecular Biology (miscellaneous) Instability Budding yeast In vitro Article 03 medical and health sciences 030104 developmental biology 0302 clinical medicine medicine.anatomical_structure Tubulin In vivo Microtubule medicine biology.protein Biophysics 030217 neurology & neurosurgery |
| Zdroj: | Life science alliance |
| ISSN: | 2575-1077 |
| Popis: | Dynamic instability is an intrinsic property of microtubules; however, we do not understand what domains of αβ-tubulins regulate this activity or how these regulate microtubule networks in cells. Here, we define a role for the negatively charged carboxy-terminal tail (CTT) domain of β-tubulin in regulating dynamic instability. By combining in vitro studies with purified mammalian tubulin and in vivo studies with tubulin mutants in budding yeast, we demonstrate that β-tubulin CTT inhibits microtubule stability and regulates the structure and stability of microtubule plus ends. Tubulin that lacks β-tubulin CTT polymerizes faster and depolymerizes slower in vitro and forms microtubules that are more prone to catastrophe. The ends of these microtubules exhibit a more blunted morphology and rapidly switch to disassembly after tubulin depletion. In addition, we show that β-tubulin CTT is required for magnesium cations to promote depolymerization. We propose that β-tubulin CTT regulates the assembly of stable microtubule ends and provides a tunable mechanism to coordinate dynamic instability with ionic strength in the cell. |
| Databáze: | OpenAIRE |
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