ArticleBiophysics (Nagoya-shi, Japan)2013
Single molecule FRET observation of kinesin-1's head-tail interaction on microtubule.
Article in Biophysics (Nagoya-shi, Japan), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Nonthermal fluctuations accelerate biomolecular motors.Biophysical reviews · 2024Review
- Evaluating the effect of two-dimensional molecular layout on DNA origami-based transporters.Nanoscale advances · 2023Article
- Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs.BMC biology · 2022Article
- Experimental and theoretical energetics of walking molecular motors under fluctuating environments.Biophysical reviews · 2020Review
- In Vitro FRET- and Fluorescence-Based Assays to Study Protein Conformation and Protein-Protein Interactions in Mitosis.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Fluorescence microscopy applied to intracellular transport by microtubule motors.Journal of biosciences · 2018Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-1 (conventional kinesin) is a molecular motor that transports various cargo such as endoplasmic reticulum and mitochondria in cells. Its two head domains walk along microtubule by hydrolyzing ATP, while the tail domains at the end of the long stalk bind to the cargo. When a kinesin is not carrying cargo, its motility and ATPase activity is inhibited by direct interactions between the tail and head. However, the mechanism of this tail regulation is not well understood. Here, we apply single molecule fluorescence resonance energy transfer (smFRET) to observe this interaction in stalk-truncated kinesin. We found that kinesin with two tails forms a folding conformation and dissociates from microtubules, whereas kinesin with one tail remains bound to the micro-tubule and is immobile even in the presence of ATP. We further investigated the head-tail interaction as well as head-head coordination on the microtubule at various nucleotide conditions. From these results, we propose a two-step inhibition model for kinesin motility.
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