ArticleProceedings of the National Academy of Sciences of the United States of America2006
The distance that kinesin-1 holds its cargo from the microtubule surface measured by fluorescence interference contrast microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 143 citations in OpenAlex.
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- Spatial confinement shapes organelle architecture and remodeling in axons.bioRxiv : the preprint server for biology · 2026Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.Molecular biology of the cell · 2025Article
- Microtubule polymerization generates microtentacles important in circulating tumor cell invasion.Biophysical journal · 2025Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.bioRxiv : the preprint server for biology · 2025Article
- A de novo designed coiled coil-based switch regulates the microtubule motor kinesin-1.Nature chemical biology · 2024Article
- A new method to experimentally quantify dynamics of initial protein-protein interactions.Communications biology · 2024Article
- In situ structure of actin remodeling during glucose-stimulated insulin secretion using cryo-electron tomography.Nature communications · 2024Article
- Exploitation of Engineered Light-Switchable Myosin XI for Nanotechnological Applications.ACS nano · 2023Article
- Cholesterol in the cargo membrane amplifies tau inhibition of kinesin-1-based transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Surface-limited reactions for spatial control of kinesin-microtubule motility assays using indirect irradiation of an electron beam.Biomicrofluidics · 2022Article
- Review
- Tuning ensemble-averaged cargo run length via fractional change in mean kinesin number.Physical biology · 2021Article
- Article
- In situ cryo-electron tomography reveals filamentous actin within the microtubule lumen.The Journal of cell biology · 2020Article
- Different motilities of microtubules driven by kinesin-1 and kinesin-14 motors patterned on nanopillars.Science advances · 2020Article
- Regulation of MT dynamics via direct binding of an Abl family kinase.The Journal of cell biology · 2019Article
- The model of local axon homeostasis - explaining the role and regulation of microtubule bundles in axon maintenance and pathology.Neural development · 2019Review
- Force Generated by Two Kinesin Motors Depends on the Load Direction and Intermolecular Coupling.Physical review letters · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-1 is a motor protein that carries cellular cargo such as membrane-bounded organelles along microtubules (MTs). The homodimeric motor molecule contains two N-terminal motor domains (the motor "heads"), a long coiled-coil domain (the "rod" or "stalk"), and two small globular "tail" domains. Much has been learned about how kinesin's heads step along a MT and how the tail is involved in cargo binding and autoinhibition. However, little is known about the role of the rod. Here, we investigate the extension of the rod during active transport by measuring the height at which MTs glide over a kinesin-coated surface in the presence of ATP. To perform height measurements with nanometer precision, we used fluorescence interference contrast microscopy, which is based on the self-interference of fluorescent light from objects near a reflecting surface. Using an in situ calibrating method, we determined that kinesin-1 molecules elevate gliding MTs 17 +/- 2 nm (mean +/- SEM) above the surface. When varying the composition of the surrounding nucleotides or removing the negatively charged -COOH termini of the MTs by subtilisin digestion, we found no significant changes in the measured distance. Even though this distance is significantly shorter than the contour length of the motor molecule ( approximately 60 nm), it may be sufficient to prevent proteins bound to the MTs or prevent the organelles from interfering with transport.
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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.