AI Article Synopsis
- Dyneins are motor proteins that use energy from ATP hydrolysis to create force and movement on microtubules, playing crucial roles in processes like ciliary beating, cell division, and intracellular transport.
- The complexity of dynein has made it challenging to understand, but advancements in techniques like X-ray crystallography and cryo-electron microscopy have helped researchers make progress.
- Current studies are revealing a model where flexing motions in dynein's AAA+ ring change how it interacts with microtubules, enabling movement through a mechanochemical cycle.
Article Abstract
Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how these giant motor proteins work. From these studies, a model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3972880 | PMC |
| http://dx.doi.org/10.1038/nrm3667 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!