Loading direction regulates the affinity of ADP for kinesin
Abstract
Kinesin is an ATP-driven molecular motor that moves processively along a microtubule. Processivity has been explained as a mechanism that involves alternating single- and double-headed binding of kinesin to microtubules coupled to the ATPase cycle of the motor. The internal load imposed between the two bound heads has been proposed to be a key factor regulating the ATPase cycle in each head. Here we show that external load imposed along the direction of motility on a single kinesin molecule enhances the binding affinity of ADP for kinesin, whereas an external load imposed against the direction of motility decreases it. This coupling between loading direction and enzymatic activity is in accord with the idea that the internal load plays a key role in the unidirectional and cooperative movement of processive motors.
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External load imposed against the direction of motility reduces ADP binding.
“external load imposed against the direction of motility reduces ADP binding (38”
From Stepping and Stretching (2003) · cites this paper as [38]
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References 30 · Cited by 119
- Authors
- Uemura, S., & Ishiwata, S.
- Affiliations
- Waseda University (JP)
- Corresponding author
- Ishiwata, Shin'ichi
- Venue
- Nature Structural & Molecular Biology
- Published
- 2003-03-17
- Volume
- 10
- Issue
- 4
- Pages
- 308-311
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W1965166916
- Cited by
- 119
- References
- 30
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 3 · 2017: 11 · 2016: 4 · 2015: 5 · 2014: 8 · 2013: 1 · 2012: 3
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- kinesin, loading direction, processivity, molecular motors, microtubules, ATPase cycle, internal load, external load
- MeSH terms
- Adenosine Diphosphate, Animals, Biophysics, Cattle, Kinetics, Microtubules, Models, Biological, Kinesins, Molecular Motor Proteins, Sus scrofa, Biophysical Phenomena, In Vitro Techniques
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