ArticleBiophysical reviews2011
A seesaw model for intermolecular gating in the kinesin motor protein.
Article in Biophysical reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Microtubule association induces a Mg-free apo-like ADP pre-release conformation in kinesin-1 that is unaffected by its autoinhibitory tail.Nature communications · 2025Article
- Distinct Clinical Phenotypes in KIF1A-Associated Neurological Disorders Result from Different Amino Acid Substitutions at the Same Residue in KIF1A.Biomolecules · 2025Article
- Kinetic regulation of kinesin's two motor domains coordinates its stepping along microtubules.eLife · 2025Article
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.Open biology · 2023Article
- A neuropathy-associated kinesin KIF1A mutation hyper-stabilizes the motor-neck interaction during the ATPase cycle.The EMBO journal · 2022Article
- Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14.Nature communications · 2021Article
- 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
- Shaft Function of Kinesin-1's α4 Helix in the Processive Movement.Cellular and molecular bioengineering · 2019Article
- Article
- Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.Nature communications · 2018Article
- Anchor Effect of Interactions Between Kinesin's Nucleotide-Binding Pocket and Microtubule.Cellular and molecular bioengineering · 2017Article
- The Kinesin-1 Chemomechanical Cycle: Stepping Toward a Consensus.Biophysical journal · 2016Review
- The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinesin, 30 years later: Recent insights from structural studies.Protein science : a publication of the Protein Society · 2015Review
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- High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation.eLife · 2014Article
- Kinesin-5 allosteric inhibitors uncouple the dynamics of nucleotide, microtubule, and neck-linker binding sites.Biophysical journal · 2014Article
- Article
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1 author.
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Abstract
Recent structural observations of kinesin-1, the founding member of the kinesin group of motor proteins, have led to substantial gains in our understanding of this molecular machine. Kinesin-1, similar to many kinesin family members, assembles to form homodimers that use alternating ATPase cycles of the catalytic motor domains, or "heads", to proceed unidirectionally along its partner filament (the microtubule) via a hand-over-hand mechanism. Cryo-electron microscopy has now revealed 8-Å resolution, 3D reconstructions of kinesin-1•microtubule complexes for all three of this motor's principal nucleotide-state intermediates (ADP-bound, no-nucleotide, and ATP analog), the first time filament co-complexes of any cytoskeletal motor have been visualized at this level of detail. These reconstructions comprehensively describe nucleotide-dependent changes in a monomeric head domain at the secondary structure level, and this information has been combined with atomic-resolution crystallography data to synthesize an atomic-level "seesaw" mechanism describing how microtubules activate kinesin's ATP-sensing machinery. The new structural information revises or replaces key details of earlier models of kinesin's ATPase cycle that were based principally on crystal structures of free kinesin, and demonstrates that high-resolution characterization of the kinesin-microtubule complex is essential for understanding the structural basis of the cycle. I discuss the broader implications of the seesaw mechanism within the cycle of a fully functional kinesin dimer and show how the seesaw can account for two types of "gating" that keep the ATPase cycles of the two heads out of sync during processive movement.
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