ArticleProceedings of the National Academy of Sciences of the United States of America2006
Two modes of microtubule sliding driven by cytoplasmic dynein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 67 citations in OpenAlex.
- The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein.Nature communications · 2020Article
- Molecular mechanism of cytoplasmic dynein tension sensing.Nature communications · 2019Article
- Coupling of ATPase activity, microtubule binding, and mechanics in the dynein motor domain.The EMBO journal · 2019Article
- Nanometer-accuracy distance measurements between fluorophores at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Polarity sorting of axonal microtubules: a computational study.Molecular biology of the cell · 2017Article
- Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations.PLoS computational biology · 2017Article
- Direct observation shows superposition and large scale flexibility within cytoplasmic dynein motors moving along microtubules.Nature communications · 2015Article
- Mechanism and regulation of cytoplasmic dynein.Annual review of cell and developmental biology · 2015Review
- Dynein Heavy Chain, Encoded by Two Genes in Agaricomycetes, Is Required for Nuclear Migration in Schizophyllum commune.PloS one · 2015Article
- Article
- Tension on the linker gates the ATP-dependent release of dynein from microtubules.Nature communications · 2014Article
- Functions and mechanics of dynein motor proteins.Nature reviews. Molecular cell biology · 2013Review
- Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo.The Journal of biological chemistry · 2013Article
- ATP-driven remodeling of the linker domain in the dynein motor.Structure (London, England : 1993) · 2012Article
- Structural basis for microtubule binding and release by dynein.Science (New York, N.Y.) · 2012Article
- X-ray structure of a functional full-length dynein motor domain.Nature structural & molecular biology · 2011Article
- Communication between the AAA+ ring and microtubule-binding domain of dynein.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Opposite-polarity motors activate one another to trigger cargo transport in live cells.The Journal of cell biology · 2009Article
- Multiscale approaches for studying energy transduction in dynein.Physical chemistry chemical physics : PCCP · 2009Review
- Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells.Journal of cell science · 2009Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynein is a huge multisubunit microtubule (MT)-based motor, whose motor domain resides in the heavy chain. The heavy chain comprises a ring of six AAA (ATPases associated with diverse cellular activities) modules with two slender protruding domains, the tail and stalk. It has been proposed that during the ATP hydrolysis cycle, this tail domain swings against the AAA ring as a lever arm to generate the power stroke. However, there is currently no direct evidence to support the model that the tail swing is tightly linked to dynein motility. To address the question of whether the power stroke of the tail drives MT sliding, we devised an in vitro motility assay using genetically biotinylated cytoplasmic dyneins anchored on a glass surface in the desired orientation with a biotin-streptavidin linkage. Assays on the dyneins with the site-directed biotin tag at eight different locations provided evidence that robust MT sliding is driven by the power stroke of the tail. Furthermore, the assays revealed slow MT sliding independent of dynein orientation on the glass surface, which is mechanically distinct from the sliding driven by the power stroke of the tail.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.