Dynein is regulated by the stability of its microtubule track
| Autor: | Jeffrey K. Moore, Colby P. Fees, Cassi Estrem |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Time Factors Dynein Saccharomyces cerevisiae Spindle Apparatus macromolecular substances Biology Microtubules Article 03 medical and health sciences Dynein ATPase Microtubule Research Articles Protein Stability Cell Cycle Dyneins Microtubule organizing center Dynactin Complex Cell Biology Cell biology Spindle apparatus 030104 developmental biology Mutation Dynactin Astral microtubules Cytokinesis |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.201611105 |
| Popis: | Accurate spindle positioning depends on the action of the dynein motor protein at microtubules. Estrem et al. now show that increased dynein-mediated activity destabilizes microtubules by displacing dynactin from the plus end and suggests that the interplay between these opposing effects on microtubule stability at the cortex is required to move the spindle to the correct position. How dynein motors accurately move cargoes is an important question. In budding yeast, dynein moves the mitotic spindle to the predetermined site of cytokinesis by pulling on astral microtubules. In this study, using high-resolution imaging in living cells, we discover that spindle movement is regulated by changes in microtubule plus-end dynamics that occur when dynein generates force. Mutants that increase plus-end stability increase the frequency and duration of spindle movements, causing positioning errors. We find that dynein plays a primary role in regulating microtubule dynamics by destabilizing microtubules. In contrast, the dynactin complex counteracts dynein and stabilizes microtubules through a mechanism involving the shoulder subcomplex and the cytoskeletal-associated protein glycine-rich domain of Nip100/p150glued. Our results support a model in which dynein destabilizes its microtubule substrate by using its motility to deplete dynactin from the plus end. We propose that interplay among dynein, dynactin, and the stability of the microtubule substrate creates a mechanism that regulates accurate spindle positioning. |
| Databáze: | OpenAIRE |
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