ArticleProceedings of the National Academy of Sciences of the United States of America2011
Interhead tension determines processivity across diverse N-terminal kinesins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- Article
- Oxidative stress impairs processive motility of the axonal transport motor KIF1A.The Journal of biological chemistry · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak interhead coordination.Biophysical journal · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak inter-head coordination.bioRxiv : the preprint server for biology · 2025Article
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- Kinesin-7 CENP-E in tumorigenesis: Chromosome instability, spindle assembly checkpoint, and applications.Frontiers in molecular biosciences · 2024Review
- KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Tau differentially regulates the transport of early endosomes and lysosomes.Molecular biology of the cell · 2022Article
- Mechanistic insights into central spindle assembly mediated by the centralspindlin complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Drag-induced directionality switching of kinesin-5 Cin8 revealed by cluster-motility analysis.Science advances · 2021Article
- A kinetic dissection of the fast and superprocessive kinesin-3 KIF1A reveals a predominant one-head-bound state during its chemomechanical cycle.The Journal of biological chemistry · 2020Article
- How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.International journal of molecular sciences · 2020Review
- Leaving no-one behind: how CENP-E facilitates chromosome alignment.Essays in biochemistry · 2020Review
- Dynactin p150 promotes processive motility of DDB complexes by minimizing diffusional behavior of dynein.Molecular biology of the cell · 2020Article
- Kinesin-7 CENP-E regulates chromosome alignment and genome stability of spermatogenic cells.Cell death discovery · 2020Article
- The crowding dynamics of the motor protein kinesin-II.PloS one · 2020Article
- A Generalized Kinetic Model for Coupling between Stepping and ATP Hydrolysis of Kinesin Molecular Motors.International journal of molecular sciences · 2019Article
- Kinesin-5 Promotes Microtubule Nucleation and Assembly by Stabilizing a Lattice-Competent Conformation of Tubulin.Current biology : CB · 2019Article
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2 authors.
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Abstract
Consistent with their diverse intracellular roles, the processivity of N-terminal kinesin motors varies considerably between different families. Kinetics experiments on isolated motor domains suggest that differences in processivity result from differences in the underlying biochemistry of the catalytic heads. However, the length of the flexible neck linker domain also varies from 14 to 18 residues between families. Because the neck linker acts as a mechanical element that transmits interhead tension, altering its mechanical properties is expected to affect both front and rear head gating, mechanisms that underlie processive walking. To test the hypothesis that processivity differences result from family-specific differences in neck linker mechanics, we systematically altered the neck linker length in kinesin-1, -2, -3, -5, and -7 motors and measured run length and velocity in a single-molecule fluorescence assay. Shortening the neck linkers of kinesin-3 (Unc104/KIF1A) and kinesin-5 (Eg5/KSP) to 14 residues enhanced processivity to match kinesin-1, which has a 14-residue neck linker. After substituting a single residue in the last alpha helix of the catalytic core, kinesin-7 (CENP-E) exhibited this same behavior. This convergence of processivity was observed even though motor speeds varied over a 25-fold range. These results suggest that differences in unloaded processivity between diverse kinesins is primarily due to differences in the lengths of their neck linker domains rather than specific tuning of rate constants in their ATP hydrolysis cycles.
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