Diffusive Movement of Processive Kinesin-1 on Microtubules
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Summary
ADP can exist in a state that diffuses along the microtubule lattice without expending energy, which may facilitate the ability of kinesin to pick up cargo, and/or allow the kinesIn/cargo complex to stay bound after encountering obstacles.
- Type
- article
- Published
- 2009-06-21
- Cited by
- 57
- References
- 37
- Access
- Open access
- OpenAlex
- https://openalex.org/W1974345291
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12781256
Keywords
Kinesin, Microtubule, Biophysics, Biology, Cell biology
References
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- The kinesin-1 motor protein is regulated by a direct interaction of its head and tail
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- Motility of single one-headed kinesin molecules along microtubules.
- Intracellular imaging of targeted proteins labeled with quantum dots.
- Direct long-term observation of kinesin processivity at low load.
- The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
- Kinesin-1 structural organization and conformational changes revealed by FRET stoichiometry in live cells
- Post‐translational modifications of tubulin in the nervous system
- Tracking single Kinesin molecules in the cytoplasm of mammalian cells.
- Microtubule cross-linking triggers the directional motility of kinesin-5
- Myosin V Walks Hand-Over-Hand: Single Fluorophore Imaging with 1.5-nm Localization
- Minus-end-directed motor Ncd exhibits processive movement that is enhanced by microtubule bundling in vitro.
- Interacting Head Mechanism of Microtubule-Kinesin ATPase*
- Allosteric inhibition of kinesin-5 modulates its processive directional motility
Cited by
- Facing the environment: hydrodynamics and confinement modulate molecular motors dynamics
- Studies into molecular mechanisms of skeletal muscle contraction: Applications to transgenic mice with inherited cardiomyopathies
- Diffusion of Myosin V on Microtubules: A Fine-Tuned Interaction for Which E-Hooks Are Dispensable
- Mesoscopic analysis of motion and conformation of cross-bridges
- Transport and diffusion of Tau protein in neurons
- KIF5C, a kinesin motor involved in apical trafficking of MDCK cells
- Quantum dots find their stride in single molecule tracking
- Bidirectional cargo transport: Moving beyond tug-of-war
- Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.
- The Nucleotide-binding State of Microtubules Modulates Kinesin Processivity and the Ability of Tau to Inhibit Kinesin-mediated Transport*
- Moving into the cell: single-molecule studies of molecular motors in complex environments
- Stable Kinesin and Dynein Assemblies Drive the Axonal Transport of Mammalian Prion Protein Vesicles
- Kinesin’s light chains inhibit the head- and microtubule-binding activity of its tail
- Microtubule-based transport – basic mechanisms, traffic rules and role in neurological pathogenesis
- Processive behaviour of kinesin observed using micro-fabricated cantilevers
- Tau Protein Diffuses along the Microtubule Lattice*
- Motor Domain Phosphorylation Modulates Kinesin-1 Transport*
- Intracellular tracking of single native molecules with electroporation-delivered quantum dots.
- Kinesin-8 is a low-force motor protein with a weakly bound slip state.
- Kinetochore kinesin CENP-E is a processive bi-directional tracker of dynamic microtubule tips
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- Kinesin passing permanent blockages along its protofilament track.
- Identification of key residues that regulate the interaction of kinesins with microtubule ends
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