ArticleBiochemistry2009
Half-site inhibition of dimeric kinesin head domains by monomeric tail domains.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 58 citations in OpenAlex.
- Article
- Consequences of the Novel ALS-AssociatedNeurology. Genetics · 2026Article
- Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo.iScience · 2026Article
- 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
- Molecular architecture of the autoinhibited kinesin-1 lambda particle.Science advances · 2022Article
- ALS-linked KIF5A ΔExon27 mutant causes neuronal toxicity through gain-of-function.EMBO reports · 2022Article
- ALS-associated KIF5A mutations abolish autoinhibition resulting in a toxic gain of function.Cell reports · 2022Article
- 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
- In Vitro FRET- and Fluorescence-Based Assays to Study Protein Conformation and Protein-Protein Interactions in Mitosis.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Kinesin-dependent transport of keratin filaments: a unified mechanism for intermediate filament transport.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Coiled-coil 1-mediated fastening of the neck and motor domains for kinesin-3 autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3.Structure (London, England : 1993) · 2018Article
- An automated in vitro motility assay for high-throughput studies of molecular motors.Lab on a chip · 2018Article
- A small-molecule activator of kinesin-1 drives remodeling of the microtubule network.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Kinesin-2 motors adapt their stepping behavior for processive transport on axonemes and microtubules.EMBO reports · 2017Article
- SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain.Journal of cell science · 2017Article
- The light chains of kinesin-1 are autoinhibited.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5).Journal of molecular biology · 2016Article
- Article
- Unique function of Kinesin Kif5A in localization of mitochondria in axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The two heavy chains of kinesin-1 are dimerized through extensive coiled coil regions and fold into an inactive conformation through interaction of the C-terminal tail domains with the N-terminal motor (head) domains. Although this potentially allows a dimer of tail domains to interact symmetrically with a dimer of head domains, we report here that only one of the two available monomeric tail peptides is sufficient for tight binding and inhibition of a dimer of head domains. With a dimeric tail construct, the other tail peptide does not make tight contact with the head dimer and can bind a second head dimer to form a complex containing one tail dimer and two head dimers. The IAK domain and neighboring positively charged region of the tail is sufficient for tight half-site interaction with a dimer of heads. The interaction of tails with monomeric heads is weak, but a head dimer produced by the dimerization of the neck coil is not required because an artificial dimer of head domains also binds monomeric tail peptides with half-site stoichiometry in the complete absence of the native neck coil. The binding of tail peptides to head dimers is fast and readily reversible as determined by FRET between mant-ADP bound to the head dimer and a tail labeled with GFP. The association and dissociation rates are 81 microM(-1) s(-1) and 32 s(-1), respectively. This half-site interaction suggests that the second tail peptide in a folded kinesin-1 might be available to bind other molecules while kinesin-1 remained folded.
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