ArticleMolecular biology of the cell2004
The lipid binding pleckstrin homology domain in UNC-104 kinesin is necessary for synaptic vesicle transport in Caenorhabditis elegans.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 147 citations in OpenAlex.
- Pathogenic KIF1A variants differentially disrupt axonal trafficking and impede synaptic development.The Journal of cell biology · 2026Article
- Pathogenic KIF1A variants differentially disrupt axonal trafficking and impede synaptic development.bioRxiv : the preprint server for biology · 2026Article
- Methods to Study the Role of Cytoskeletal Motor Proteins in the Organization of the Postsynaptic Membrane.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mitochondria transported by Kinesin-3 prevent localized calcium spiking to inhibit caspase-dependent specialized cell death.Current biology : CB · 2025Article
- New insights into the influence of temperature on axonal transport and function in myelinated regions of Schwann cells.iScience · 2025Review
- The tail domain of the plant kinesin-12 POK2 is a versatile interaction hub.Journal of cell science · 2025Article
- Article
- Dynein-driven regulation of postsynaptic membrane architecture and synaptic function.Journal of cell science · 2025Article
- Polyunsaturated Fatty Acids as Potential Treatments for COVID-19-Induced Anosmia.Biomedicines · 2024Review
- Presynaptic perspective: Axonal transport defects in neurodevelopmental disorders.The Journal of cell biology · 2024Review
- F-box protein FBXB-65 regulates anterograde transport of the kinesin-3 motor UNC-104 through a PTM near its cargo-binding PH domain.Journal of cell science · 2024Article
- A plant flavonol and genetic suppressors rescue a pathogenic mutation associated with kinesin in neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Phosphatidylinositol 3,5-bisphosphate facilitates axonal vesicle transport and presynapse assembly.Science (New York, N.Y.) · 2023Article
- End-binding protein 1 promotes specific motor-cargo association in the cell body prior to axonal delivery of dense core vesicles.Current biology : CB · 2023Article
- Presynaptic Precursor Vesicles-Cargo, Biogenesis, and Kinesin-Based Transport across Species.Cells · 2023Review
- End Binding protein 1 promotes specific motor-cargo association in the cell body prior to axonal delivery of Dense Core Vesicles.bioRxiv : the preprint server for biology · 2023Article
- Selective motor activation in organelle transport along axons.Nature reviews. Molecular cell biology · 2022Review
- De novo mutations in KIF1A-associated neuronal disorder (KAND) dominant-negatively inhibit motor activity and axonal transport of synaptic vesicle precursors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Specific KIF1A-adaptor interactions control selective cargo recognition.The Journal of cell biology · 2021Article
- Automated segmentation and tracking of mitochondria in live-cell time-lapse images.Nature methods · 2021Article
19 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
UNC-104 (KIF1A) is a kinesin motor that transports synaptic vesicles from the neuronal cell body to the terminal. Previous in vitro studies have shown that a Dictyostelium relative of UNC-104 transports liposomes containing acidic phospholipids, but whether this interaction is needed for the recognition and transport of synaptic vesicles in metazoans remains unexplored. Here, we have introduced mutations in the nonmotor domain of UNC-104 and examined whether these mutant motors can rescue an unc-104 Caenorhabditis elegans strain. We show that a pleckstrin homology (PH) domain in UNC-104 is essential for membrane transport in living C. elegans, that this PH domain binds specifically to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2)), and that point mutants in the PH domain that interfere with PI(4,5)P(2) binding in vitro also interfere with UNC-104 function in vivo. Several other lipid-binding modules could not effectively substitute for the UNC-104 PH domain in this in vivo assay. Real time imaging also revealed that a lipid-binding point mutation in the PH domain reduced movement velocity and processivity of individual UNC-104::GFP punctae in neurites. These results reveal a critical role for PI(4,5)P(2) binding in UNC-104-mediated axonal transport and shows that the cargo-binding properties of the distal PH domain can affect motor output.
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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.