ArticleProceedings of the National Academy of Sciences of the United States of America2008
The kinesin-1 motor protein is regulated by a direct interaction of its head and tail.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 132 citations in OpenAlex.
- Structural basis of kinesin-1 autoinhibition and its control of microtubule-based motility.Science advances · 2026Article
- Article
- Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo.iScience · 2026Article
- What Determines the Directionality of Kinesins? Studying the Anomalous Directionality of Nonclaret Disjunctional Motor Mutants.Journal of the American Chemical Society · 2026Article
- Phosphorylation-dependent regional motility of the ciliary kinesin OSM-3.The Journal of cell biology · 2025Article
- 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
- Article
- Optogenetic control of kinesin-1, -2, -3 and dynein reveals their specific roles in vesicular transport.Cell reports · 2024Article
- Unraveling the interplay of kinesin-1, tau, and microtubules in neurodegeneration associated with Alzheimer's disease.Frontiers in cellular neuroscience · 2024Review
- Article
- Article
- Unravelling the mechanotransduction pathways in Alzheimer's disease.Journal of biological engineering · 2023Review
- Kinesin-1 autoinhibition facilitates the initiation of dynein cargo transport.The Journal of cell biology · 2023Article
- Molecular architecture of the autoinhibited kinesin-1 lambda particle.Science advances · 2022Article
- ALS-linked KIF5A ΔExon27 mutant causes neuronal toxicity through gain-of-function.EMBO reports · 2022Article
- Synergistic autoinhibition and activation mechanisms control kinesin-1 motor activity.Cell reports · 2022Article
- ALS-associated KIF5A mutations abolish autoinhibition resulting in a toxic gain of function.Cell reports · 2022Article
- Resolving kinesin stepping: one head at a time.Life science alliance · 2019Article
- MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules.The Journal of biological chemistry · 2019Article
- GTP-binding facilitates EB1 recruitment onto microtubules by relieving its auto-inhibition.Scientific reports · 2018Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Kinesin-1 is a molecular motor protein that transports cargo along microtubules. Inside cells, the vast majority of kinesin-1 is regulated to conserve ATP and to ensure its proper intracellular distribution and coordination with other molecular motors. Regulated kinesin-1 folds in half at a hinge in its coiled-coil stalk. Interactions between coiled-coil regions near the enzymatically active heads at the N terminus and the regulatory tails at the C terminus bring these globular elements in proximity and stabilize the folded conformation. However, it has remained a mystery how kinesin-1's microtubule-stimulated ATPase activity is regulated in this folded conformation. Here, we present evidence for a direct interaction between the kinesin-1 head and tail. We photochemically cross-linked heads and tails and produced an 8-A cryoEM reconstruction of the cross-linked head-tail complex on microtubules. These data demonstrate that a conserved essential regulatory element in the kinesin-1 tail interacts directly and specifically with the enzymatically critical Switch I region of the head. This interaction suggests a mechanism for tail-mediated regulation of the ATPase activity of kinesin-1. In our structure, the tail makes simultaneous contacts with the kinesin-1 head and the microtubule, suggesting the tail may both regulate kinesin-1 in solution and hold it in a paused state with high ADP affinity on microtubules. The interaction of the Switch I region of the kinesin-1 head with the tail is strikingly similar to the interactions of small GTPases with their regulators, indicating that other kinesin motors may share similar regulatory mechanisms.
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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.