ReviewProtein science : a publication of the Protein Society2015
Kinesin, 30 years later: Recent insights from structural studies.
Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.
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Who cites it
31 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.
- Prognostic and clinicopathological significance of kinesin family member C1 in various cancers: A meta-analysis.Medicine · 2019Pooled it
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- A conserved minimal core and modular extensions make the fungal flagellum.Scientific reports · 2026Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Lowering Ionic Strength Improves the Sensitivity of Microtubule Gliding Assay Based Molecular Detection.Nano letters · 2025Article
- Interaction of Tau with Kinesin-1: Effect of Kinesin-1 Heavy Chain Elimination on Autophagy-Mediated Mutant Tau Degradation.Biomedicines · 2023Article
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- Causes, costs and consequences of kinesin motors communicating through the microtubule lattice.Journal of cell science · 2023Article
- Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022Review
- Biological functions and potential therapeutic applications of huntingtin-associated protein 1: progress and prospects.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022Review
- KIF13A-A Key Regulator of Recycling Endosome Dynamics.Frontiers in cell and developmental biology · 2022Review
- Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding.Science advances · 2021Article
- Neurogenomic divergence during speciation by reinforcement of mating behaviors in chorus frogs (Pseudacris).BMC genomics · 2021Article
- Structural snapshots of the kinesin-2 OSM-3 along its nucleotide cycle: implications for the ATP hydrolysis mechanism.FEBS open bio · 2021Article
- The developmental biology of kinesins.Developmental biology · 2021Review
- Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020Review
- How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.International journal of molecular sciences · 2020Review
- Synthetic biology approaches to dissecting linear motor protein function: towards the design and synthesis of artificial autonomous protein walkers.Biophysical reviews · 2020Review
- Anterograde Axonal Transport in Neuronal Homeostasis and Disease.Frontiers in molecular neuroscience · 2020Review
- Building machines with DNA molecules.Nature reviews. Genetics · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Motile kinesins are motor proteins that move unidirectionally along microtubules as they hydrolyze ATP. They share a conserved motor domain (head) which harbors both the ATP- and microtubule-binding activities. The kinesin that has been studied most moves toward the microtubule (+)-end by alternately advancing its two heads along a single protofilament. This kinesin is the subject of this review. Its movement is associated to alternate conformations of a peptide, the neck linker, at the C-terminal end of the motor domain. Recent progress in the understanding of its structural mechanism has been made possible by high-resolution studies, by cryo electron microscopy and X-ray crystallography, of complexes of the motor domain with its track protein, tubulin. These studies clarified the structural changes that occur as ATP binds to a nucleotide-free microtubule-bound kinesin, initiating each mechanical step. As ATP binds to a head, it triggers orientation changes in three rigid motor subdomains, leading the neck linker to dock onto the motor core, which directs the other head toward the microtubule (+)-end. The relationship between neck linker docking and the orientations of the motor subdomains also accounts for kinesin's processivity, which is remarkable as this motor protein only falls off from a microtubule after taking about a hundred steps. As tools are now available to determine high-resolution structures of motor domains complexed to their track protein, it should become possible to extend these studies to other kinesins and relate their sequence variations to their diverse properties.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.