ArticleMolecular biology of the cell2014
The family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Synthetic cargo adaptors reveal molecular features that enhance dynein activation.Nature communications · 2026Article
- Article
- Stall force measurement of the kinesin-3 motor KIF1A using a programmable DNA origami nanospring.eLife · 2026Article
- Kinesin-1 autoinhibition tunes cargo transport by motor ensembles.Biophysical journal · 2025Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- The alpha tubulin acetyltransferasemicroPublication biology · 2025Article
- Poxvirus A51R Proteins Negatively Regulate Microtubule-Dependent Transport by Kinesin-1.International journal of molecular sciences · 2024Article
- Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.Nature communications · 2024Article
- A Model for Chemomechanical Coupling of Kinesin-3 Motor.Cellular and molecular bioengineering · 2024Article
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- KIF1A-Associated Neurological Disorder: An Overview of a Rare Mutational Disease.Pharmaceuticals (Basel, Switzerland) · 2023Review
- 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
- Microtubule lattice spacing governs cohesive envelope formation of tau family proteins.Nature chemical biology · 2022Article
- Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.BMC biology · 2022Article
- KIF13A-A Key Regulator of Recycling Endosome Dynamics.Frontiers in cell and developmental biology · 2022Review
- Genotype and defects in microtubule-based motility correlate with clinical severity inHGG advances · 2021Article
- Pathogenic mutations in the kinesin-3 motor KIF1A diminish force generation and movement through allosteric mechanisms.The Journal of cell biology · 2021Article
- A highly conserved 3Science 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
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2 authors.
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Abstract
The kinesin-3 family (KIF) is one of the largest among the kinesin superfamily and an important driver of a variety of cellular transport events. Whereas all kinesins contain the highly conserved kinesin motor domain, different families have evolved unique motor features that enable different mechanical and functional outputs. A defining feature of kinesin-3 motors is the presence of a positively charged insert, the K-loop, in loop 12 of their motor domains. However, the mechanical and functional output of the K-loop with respect to processive motility of dimeric kinesin-3 motors is unknown. We find that, surprisingly, the K-loop plays no role in generating the superprocessive motion of dimeric kinesin-3 motors (KIF1, KIF13, and KIF16). Instead, we find that the K-loop provides kinesin-3 motors with a high microtubule affinity in the motor's ADP-bound state, a state that for other kinesins binds only weakly to the microtubule surface. A high microtubule affinity results in a high landing rate of processive kinesin-3 motors on the microtubule surface. We propose that the family-specific K-loop contributes to efficient kinesin-3 cargo transport by enhancing the initial interaction of dimeric motors with the microtubule track.
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