ArticleBiophysical journal2009
The Kinesin-1 tail conformationally restricts the nucleotide pocket.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail.Nature communications · 2025Article
- Kinesin-1 autoinhibition facilitates the initiation of dynein cargo transport.The Journal of cell biology · 2023Article
- Resolving kinesin stepping: one head at a time.Life science alliance · 2019Article
- SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain.Journal of cell science · 2017Article
- The light chains of kinesin-1 are autoinhibited.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- The actin-microtubule cross-linking activity of Drosophila Short stop is regulated by intramolecular inhibition.Molecular biology of the cell · 2013Article
- Single molecule FRET observation of kinesin-1's head-tail interaction on microtubule.Biophysics (Nagoya-shi, Japan) · 2013Article
- Three routes to suppression of the neurodegenerative phenotypes caused by kinesin heavy chain mutations.Genetics · 2012Article
- Sunday Driver/JIP3 binds kinesin heavy chain directly and enhances its motility.The EMBO journal · 2011Article
- Nucleotide pocket thermodynamics measured by EPR reveal how energy partitioning relates myosin speed to efficiency.Journal of molecular biology · 2011Article
- Kinesin-1 tail autoregulation and microtubule-binding regions function in saltatory transport but not ooplasmic streaming.Development (Cambridge, England) · 2011Article
- Article
- Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The conserved L5 loop establishes the pre-powerstroke conformation of the Kinesin-5 motor, eg5.Biophysical journal · 2010Article
- Herpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Journal of virology · 2010Article
- Traffic control: regulation of kinesin motors.Nature reviews. Molecular cell biology · 2009Review
- Kinesin superfamily motor proteins and intracellular transport.Nature reviews. Molecular cell biology · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We have used electron paramagnetic resonance and fluorescence spectroscopy to study the interaction between the kinesin-1 head and its regulatory tail domain. The interaction between the tails and the enzymatically active heads has been shown to inhibit intrinsic and microtubule-stimulated ADP release. Here, we demonstrate that the probe mobility of two different spin-labeled nucleotide analogs in the kinesin-1 nucleotide pocket is restricted upon binding of the tail domain to kinesin-1 heads. This conformational restriction is distinct from the microtubule-induced changes in the nucleotide pocket. Unlike myosin V, this tail-induced restriction occurs independent of nucleotide state. We find that the head-tail interaction that causes the restriction only weakly stabilizes Mg(2+) in the nucleotide pocket. The conformational restriction also occurs when a tail construct containing a K922A point mutation is used. This mutation eliminates the tail's ability to inhibit ADP release, indicating that the tail does not inhibit nucleotide ejection from the pocket by simple steric hindrance. Together, our data suggest that the observed head-tail interaction serves as a scaffold to position K922 to exert its inhibitory effect, possibly by interacting with the nucleotide alpha/beta-phosphates in a manner analogous to the arginine finger regulators of some G proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.