AI Article Synopsis
- Dynein is an important microtubule motor that moves toward the minus end of microtubules and is vital for various cellular functions.
- Recent advancements have improved our understanding of dynein's structure, how it changes shape during ATP hydrolysis, and the coordination of its motor domains.
- The challenges of studying dynein stem from its large size and the difficulties in creating and purifying mutant versions of the protein.
Article Abstract
Dynein is a minus-end-directed microtubule motor crucial to diverse cellular processes. The unwieldy size of the molecule and the difficulty of expressing and purifying mutants have hampered mechanistic studies of dynein. Recent progress sheds light on key unsolved questions concerning how the molecule is really organized, what conformational changes accompany ATP hydrolysis and whether two or three motor domains are coordinated in their motion.
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| http://dx.doi.org/10.1016/j.ceb.2004.12.006 | DOI Listing |
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