Mammalian end binding proteins control persistent microtubule growth
| Autor: | Marileen Dogterom, Srinivas Honnappa, Ilya Grigoriev, Christian O. De Groot, Yulia Komarova, Joseph M. Schober, Anna Akhmanova, Rubén M. Buey, E. Laura Munteanu, Susana Montenegro Gouveia, Casper C. Hoogenraad, Michel O. Steinmetz, Gary G. Borisy |
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| Přispěvatelé: | Cell biology, Neurosciences |
| Rok vydání: | 2009 |
| Předmět: |
Microtubule-associated protein
CHO Cells Plasma protein binding Biology Calponin homology domain Microtubules DNA-binding protein Article 03 medical and health sciences Cricetulus 0302 clinical medicine Protein structure Microtubule Cricetinae Animals Humans Microtubule end Research Articles 030304 developmental biology 0303 health sciences Cell Differentiation Cell Biology Protein Structure Tertiary Cell biology Tubulin biology.protein Protein Multimerization Dimerization Microtubule-Associated Proteins 030217 neurology & neurosurgery |
| Zdroj: | Journal of Cell Biology, 184(5), 691-706. Rockefeller University Press The Journal of Cell Biology The Journal of cell biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | End binding proteins (EBs) are highly conserved core components of microtubule plus-end tracking protein networks. Here we investigated the roles of the three mammalian EBs in controlling microtubule dynamics and analyzed the domains involved. Protein depletion and rescue experiments showed that EB1 and EB3, but not EB2, promote persistent microtubule growth by suppressing catastrophes. Furthermore, we demonstrated in vitro and in cells that the EB plus-end tracking behavior depends on the calponin homology domain but does not require dimer formation. In contrast, dimerization is necessary for the EB anti-catastrophe activity in cells; this explains why the EB1 dimerization domain, which disrupts native EB dimers, exhibits a dominant-negative effect. When microtubule dynamics is reconstituted with purified tubulin, EBs promote rather than inhibit catastrophes, suggesting that in cells EBs prevent catastrophes by counteracting other microtubule regulators. This probably occurs through their action on microtubule ends, because catastrophe suppression does not require the EB domains needed for binding to known EB partners. |
| Databáze: | OpenAIRE |
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