ArticleProteins2012
Kinesin tail domains are intrinsically disordered.
Article in Proteins, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Microtubule Engagement by the WD40-Containing Tail of Kinesin-4 KIF21B.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of kinesin-1 autoinhibition and its control of microtubule-based motility.Science advances · 2026Article
- Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo.iScience · 2026Article
- ALS Mutations Shift the Isoelectric Point of the KIF5A C Terminal Inducing Protein Aggregation and TDP-43 Mislocalization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- KIF3A tail domain phosphorylation is not required for ciliogenesis in mouse embryonic fibroblasts.iScience · 2024Article
- Kinesin-7 CENP-E in tumorigenesis: Chromosome instability, spindle assembly checkpoint, and applications.Frontiers in molecular biosciences · 2024Review
- Article
- Synergistic autoinhibition and activation mechanisms control kinesin-1 motor activity.Cell reports · 2022Article
- Cdt1 stabilizes kinetochore-microtubule attachments via an Aurora B kinase-dependent mechanism.The Journal of cell biology · 2018Article
- Probing Mitotic CENP-E Kinesin with the Tethered Cargo Motion Assay and Laser Tweezers.Biophysical journal · 2018Article
- Prime movers: the mechanochemistry of mitotic kinesins.Nature reviews. Molecular cell biology · 2014Review
- Novel septin 9 repeat motifs altered in neuralgic amyotrophy bind and bundle microtubules.The Journal of cell biology · 2013Article
- Delineation of the TRAK binding regions of the kinesin-1 motor proteins.FEBS letters · 2013Article
- Intrinsic Disorder in the Kinesin Superfamily.Biophysical reviews · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Kinesin motor proteins transport a wide variety of molecular cargoes in a spatially and temporally regulated manner. Kinesin motor domains, which hydrolyze ATP to produce a directed mechanical force along a microtubule, are well conserved throughout the entire superfamily. Outside of the motor domains, kinesin sequences diverge along with their transport functions. The nonmotor regions, particularly the tails, respond to a wide variety of structural and molecular cues that enable kinesins to carry specific cargoes in response to particular cellular signals. Here, we demonstrate that intrinsic disorder is a common structural feature of kinesins. A bioinformatics survey of the full-length sequences of all 43 human kinesins predicts that significant regions of intrinsically disordered residues are present in all kinesins. These regions are concentrated in the nonmotor domains, particularly in the tails and near sites for ligand binding or post-translational modifications. In order to experimentally verify these predictions, we expressed and purified the tail domains of kinesins representing three different families (Kif5B, Kif10, and KifC3). Circular dichroism and NMR spectroscopy experiments demonstrate that the isolated tails are disordered in vitro, yet they retain their functional microtubule-binding activity. On the basis of these results, we propose that intrinsic disorder is a common structural feature that confers functional specificity to kinesins.
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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.