ArticleProceedings of the National Academy of Sciences of the United States of America2010
Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Selective targeting of kinesin on lipid droplets in the liver reduces plasma lipids.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Rules of the road: how to turn off kinesin motors.The Biochemical journal · 2026Review
- The KASH protein UNC-83 differentially regulates kinesin-1 activity to control developmental stage-specific nuclear migration.Current biology : CB · 2025Article
- Unraveling the interplay of kinesin-1, tau, and microtubules in neurodegeneration associated with Alzheimer's disease.Frontiers in cellular neuroscience · 2024Review
- Article
- Glycogen synthase kinase 3β (GSK3β) and presenilin (PS) are key regulators of kinesin-1-mediated cargo motility within axons.Frontiers in cell and developmental biology · 2023Review
- How neurons maintain their axons long-term: an integrated view of axon biology and pathology.Frontiers in neuroscience · 2023Review
- Article
- ALS-associated KIF5A mutations abolish autoinhibition resulting in a toxic gain of function.Cell reports · 2022Article
- FRA1 Kinesin Modulates the Lateral Stability of Cortical Microtubules through Cellulose Synthase-Microtubule Uncoupling Proteins.The Plant cell · 2020Article
- Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- mTOR Senses Intracellular pH through Lysosome Dispersion from RHEB.BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Kinesin-1 Regulates Extrasynaptic Targeting of NMDARs and Neuronal Vulnerability Toward Excitotoxicity.iScience · 2019Article
- Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3.Structure (London, England : 1993) · 2018Article
- A New Calmodulin-Binding Protein Expresses in the Context of Secondary Cell Wall Biosynthesis and Impacts Biomass Properties inFrontiers in plant science · 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
- Native kinesin-1 does not bind preferentially to GTP-tubulin-rich microtubules in vitro.Cytoskeleton (Hoboken, N.J.) · 2017Article
- SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain.Journal of cell science · 2017Article
- The Kinesin Adaptor Calsyntenin-1 Organizes Microtubule Polarity and Regulates Dynamics during Sensory Axon Arbor Development.Frontiers in cellular neuroscience · 2017Article
- Role of kinesin-1-based microtubule sliding in Drosophila nervous system development.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kinesin-1 is a microtubule-based motor comprising two heavy chains (KHCs) and two light chains (KLCs). Motor activity is precisely regulated to avoid futile ATP consumption and to ensure proper intracellular localization of kinesin-1 and its cargoes. The KHC tail inhibits ATPase activity by interacting with the enzymatic KHC heads, and the tail also binds microtubules. Here, we present a role for the KLCs in regulating both the head- and microtubule-binding activities of the kinesin-1 tail. We show that KLCs reduce the affinity of the head-tail interaction over tenfold and concomitantly repress the tail's regulatory activity. We also show that KLCs inhibit tail-microtubule binding by a separate mechanism. Inhibition of head-tail binding requires steric and electrostatic factors. Inhibition of tail-microtubule binding is largely electrostatic, pH dependent, and mediated partly by a highly negatively charged linker region between the KHC-interacting and cargo-binding domains of the KLCs. Our data support a model wherein KLCs promote activation of kinesin-1 for cargo transport by simultaneously suppressing tail-head and tail-microtubule interactions. KLC-mediated inhibition of tail-microtubule binding may also influence diffusional movement of kinesin-1 on microtubules, and kinesin-1's role in microtubule transport/sliding.
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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.