Review: Mechanochemistry of the kinesin‐1 ATPase

Cross, Robert A.

doi:10.1002/bip.22862

Cited by 82 publications

(78 citation statements)

References 41 publications

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“…It is built up based mainly on three pieces of experimental and computational evidence and/or arguments. (a) The experimental data showed that the kinesin head in the nucleotide-free, ATP, or ADP.P i state has a strong interaction with MT, whereas in the ADP state, it has a weak interaction [39][40][41][42][43][44]. The structural data showed that the strong interaction of MT tubulin heterodimer with the kinesin head in the strong MT-binding state induces large conformational changes in the tubulin heterodimer [45].…”

Section: The Modelmentioning

confidence: 99%

Processivity of dimeric kinesin‐1 molecular motors

et al. 2018

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Kinesin‐1 is a homodimeric motor protein that can move along microtubule filaments by hydrolyzing ATP with a high processivity. How the two motor domains are coordinated to achieve such high processivity is not clear. To address this issue, we computationally studied the run length of the dimer with our proposed model. The computational data quantitatively reproduced the puzzling experimental data, including the dramatically asymmetric character of the run length with respect to the direction of external load acting on the coiled‐coil stalk, the enhancement of the run length by addition of phosphate, and the contrary features of the run length for different types of kinesin‐1 with extensions of their neck linkers compared with those without extension of the neck linker. The computational data on other aspects of the movement dynamics such as velocity and durations of one‐head‐bound and two‐head‐bound states in a mechanochemical coupling cycle were also in quantitative agreement with the available experimental data. Moreover, predicted results are provided on dependence of the run length upon external load acting on one head of the dimer, which can be easily tested in the future using single‐molecule optical trapping assays.

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Section: The Modelmentioning

confidence: 99%

Processivity of dimeric kinesin‐1 molecular motors

et al. 2018

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“…Conventional kinesin (kinesin‐1) is a motor protein having two identical N‐terminal heads connected together by a coiled‐coil stalk through their neck linkers (NLs) . The motor can move processively on microtubule (MT) protofilaments toward the plus end by hydrolyzing ATP.…”

Section: Introductionmentioning

confidence: 99%

All‐atom molecular dynamics simulations reveal how kinesin transits from one‐head‐bound to two‐heads‐bound state

et al. 2019

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Kinesin dimer walks processively along a microtubule (MT) protofilament in a hand‐over‐hand manner, transiting alternately between one‐head‐bound (1HB) and two‐heads‐bound (2HB) states. In 1HB state, one head bound by adenosine diphosphate (ADP) is detached from MT and the other head is bound to MT. Here, using all‐atom molecular dynamics simulations we determined the position and orientation of the detached ADP‐head relative to the MT‐bound head in 1HB state. We showed that in 1HB state when the MT‐bound head is in ADP or nucleotide‐free state, with its neck linker being undocked, the detached ADP‐head and the MT‐bound head have the high binding energy, and after adenosine triphosphate (ATP) binds to the MT‐bound head, with its neck linker being docked, the binding energy between the two heads is reduced greatly. These results reveal how the kinesin dimer retains 1HB state before ATP binding and how the dimer transits from 1HB to 2HB state after ATP binding. Key residues involved in the head‐head interaction in 1HB state were identified.

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“…The ATP hydrolysis cycle is coupled to conformational changes within the motor and neck domains that result in forward movement of the tail attached cargo. ATP turnover drives a sequence of conformational changes that cyclically change the microtubule binding affinity of the motor domains [1]. Kinesin motors exist in all eukaryotes and have been divided into 15 families based on the position and sequence homology of their motor domain [2,3].…”

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confidence: 99%

Intracellular cargo transport by kinesin-3 motors

Siddiqui

Straube

2017

Biochemistry Moscow

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Abstract-Intracellular transport along microtubules enables cellular cargoes to efficiently reach the extremities of large, eukaryotic cells. While it would take more than 200 years for a small vesicle to diffuse from the cell body to the growing tip of a one meter long axon, transport by a kinesin allows delivery in one week. It is clear from this example that the evolution of intracellular transport was tightly linked to the development of complex and macroscopic life forms. The human genome encodes 45 kinesins, 8 of those belonging to the family of kinesin 3 organelle transporters that are known to transport a vari ety of cargoes towards the plus end of microtubules. However, their mode of action, their tertiary structure, and regulation are controversial. In this review, we summarize the latest developments in our understanding of these fascinating molecular motors.

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Review: Mechanochemistry of the kinesin‐1 ATPase

Cited by 82 publications

References 41 publications

Processivity of dimeric kinesin‐1 molecular motors

Processivity of dimeric kinesin‐1 molecular motors

All‐atom molecular dynamics simulations reveal how kinesin transits from one‐head‐bound to two‐heads‐bound state

Intracellular cargo transport by kinesin-3 motors

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