ArticleScientific reports2012
Neck-motor interactions trigger rotation of the kinesin stalk.
Article in Scientific reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
6 citing papers in PubMed.
- Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility.Scientific reports · 2026Article
- A neuropathy-associated kinesin KIF1A mutation hyper-stabilizes the motor-neck interaction during the ATPase cycle.The EMBO journal · 2022Article
- Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding.Science advances · 2021Article
- Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein.Scientific reports · 2017Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Altered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutant.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated - neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released, and alter motor affinity for microtubules. A new structural pathway accounts for the coupling of stalk rotation - the force-producing stroke - to changes in motor affinity for nucleotide and microtubules. Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states.
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Registered trials
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