ArticleNature communications2024
Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Pathogenic KIF1A variants differentially disrupt axonal trafficking and impede synaptic development.The Journal of cell biology · 2026Article
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- KIF1A-mediated trafficking is required for neuronal autophagy in human neurons.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of kinesin-1 autoinhibition and its control of microtubule-based motility.Science advances · 2026Article
- KLP-6 is a kinesin superfamily protein resistant to ADP inhibition.Communications biology · 2026Article
- Pathogenic KIF1A R350 mutations disrupt a conserved and conformation-dependent kinesin-tubulin salt bridge.Nature communications · 2026Article
- ATPγS substantially defeats the biasing mechanism for kinesin steps.Nature communications · 2026Article
- Pathogenic KIF1A variants differentially disrupt axonal trafficking and impede synaptic development.bioRxiv : the preprint server for biology · 2026Article
- Structure and mechanism of microtubule stabilization and motor regulation by MAP9.bioRxiv : the preprint server for biology · 2025Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching.Nature communications · 2025Article
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- Distinct Clinical Phenotypes in KIF1A-Associated Neurological Disorders Result from Different Amino Acid Substitutions at the Same Residue in KIF1A.Biomolecules · 2025Article
- Molecular Motors in Myelination and Their Misregulation in Disease.Molecular neurobiology · 2025Review
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Biased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model.Biophysical journal · 2025Article
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Abstract
Mutations in the microtubule-associated motor protein KIF1A lead to severe neurological conditions known as KIF1A-associated neurological disorders (KAND). Despite insights into its molecular mechanism, high-resolution structures of KIF1A-microtubule complexes remain undefined. Here, we present 2.7-3.5 Å resolution structures of dimeric microtubule-bound KIF1A, including the pathogenic P305L mutant, across various nucleotide states. Our structures reveal that KIF1A binds microtubules in one- and two-heads-bound configurations, with both heads exhibiting distinct conformations with tight inter-head connection. Notably, KIF1A's class-specific loop 12 (K-loop) forms electrostatic interactions with the C-terminal tails of both α- and β-tubulin. The P305L mutation does not disrupt these interactions but alters loop-12's conformation, impairing strong microtubule-binding. Structure-function analysis reveals the K-loop and head-head coordination as major determinants of KIF1A's superprocessive motility. Our findings advance the understanding of KIF1A's molecular mechanism and provide a basis for developing structure-guided therapeutics against KAND.
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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 Socratic graph.