ArticleThe Journal of biological chemistry2022
A mechanochemical model of the forward/backward movement of motor protein kinesin-1.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 8 citations in OpenAlex.
- Post-translational modification-regulating biomaterials for regeneration.Bioactive materials · 2026Review
- Map-1a regulates Sertoli cell BTB dynamics through the cytoskeletal organization of microtubule and F-actin.Reproductive biology and endocrinology : RB&E · 2024Article
- Interaction of Tau with Kinesin-1: Effect of Kinesin-1 Heavy Chain Elimination on Autophagy-Mediated Mutant Tau Degradation.Biomedicines · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Kinesin-1 is an ATP-driven, two-headed motor protein that transports intracellular cargoes (loads) along microtubules. The movement of kinesin-1 has generally been modeled according to its correlation with ATP cleavage (forward movement), synthesis (backward movement), or unproductive cleavage (futile consumption). Based on recent experimental observations, we formulate a mechanochemical model for this movement in which the forward/backward/futile cycle can be realized through multiple biochemical pathways. Our results show that the backward motion of kinesin-1 occurs mainly through backward sliding along the microtubule and is usually also coupled with ATP hydrolysis. We also found that with a low external load, about 80% of ATP is wasted (futile consumption) by kinesin-1. Furthermore, at high ATP concentrations or under high external loads, both heads of kinesin-1 are always in the ATP- or ADP ⋅ Pi-binding state and tightly bound to the microtubule, while at low ATP concentrations and low loads, kinesin-1 is mainly in the one-head-bound state. Unless the external load is near the stall force, the motion of kinesin-1 is almost deterministic.
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