Data for "Motor Clustering Enhances Kinesin-driven Vesicle Transport"

Intracellular vesicles are typically transported by a small number of kinesin and dynein motors. However, the slow microtubule binding rate of kinesin-1 observed in in vitro biophysical studies suggests that long-range transport may require a high number of motors. To address the discrepancy in motor requirements between in vivo and in vitro studies, we reconstituted motility of 120-nm-diameter liposomes driven by multiple GFP-labeled kinesin-1 motors. Consistent with predictions based on previous binding rate measurements, we found that long-distance transport requires a high number of kinesin-1 motors. We hypothesized that this discrepancy from in vivo observations may arise from differences in motor organization and tested whether motor clustering can enhance transport efficiency using a DNA scaffold. Clustering just three motors increased liposome travel distances across a wide range of motor numbers. Our findings demonstrate that, independent of motor number, the arrangement of motors on a vesicle regulates transport distance, suggesting that differences in motor organization may explain the disparity between in vivo and in vitro motor requirements for long-range transport.

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Hancock, William O.; Jiang, Rui (2025). Data for "Motor Clustering Enhances Kinesin-driven Vesicle Transport" [Data set]. Scholarsphere. https://doi.org/10.26207/becz-me75

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Work Title Data for "Motor Clustering Enhances Kinesin-driven Vesicle Transport"
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Open Access
Creators
  1. William O. Hancock
  2. Rui Jiang
License CC BY-NC 4.0 (Attribution-NonCommercial)
Work Type Dataset
Acknowledgments
  1. We are grateful to Adheshwari Ramesh for her help with molecular biology of the K406GFP-SNAP construct, Ekaterina Bazilevskaya at the Penn State Materials Characterization Lab for her help with the dynamic light scattering (DLS) measurement, members of the Hancock laboratory for helpful discussions. This work was funded by NIH Grant R35GM139568. R.J. was supported by NIH Grant T32 GM108563.
Publication Date May 5, 2025
DOI doi:10.26207/becz-me75
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Deposited May 01, 2025

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Version 1
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  • Created
  • Updated
  • Updated Publisher, Description, Publication Date Show Changes
    Publisher
    • Biophysical Journal
    Description
    • Intracellular vesicles are typically transported by a small number of kinesin and dynein motors. However, the slow microtubule binding rate of kinesin-1 observed in in vitro biophysical studies suggests that long-range transport may require a high number of motors. To address the discrepancy in motor requirements between in vivo and in vitro studies, we reconstituted motility of 120-nm-diameter liposomes driven by multiple GFP-labeled kinesin-1 motors. Consistent with predictions based on previous binding rate measurements, we found that long-distance transport requires a high number of kinesin-1 motors. We hypothesized that this discrepancy from in vivo observations may arise from differences in motor organization and tested whether motor clustering can enhance transport efficiency using a DNA scaffold. Clustering just three motors increased liposome travel distances across a wide range of motor numbers. Our findings demonstrate that, independent of motor number, the arrangement of motors on a vesicle regulates transport distance, suggesting that differences in motor organization may explain the disparity between in vivo and in vitro motor requirements for long-range transport.
    Publication Date
    • 2025
  • Updated Acknowledgments Show Changes
    Acknowledgments
    • We are grateful to Adheshwari Ramesh for her help with molecular biology of the K406GFP-SNAP construct, Ekaterina Bazilevskaya at the Penn State Materials Characterization Lab for her help with the dynamic light scattering (DLS) measurement, members of the Hancock laboratory for helpful discussions. This work was funded by NIH Grant R35GM139568. R.J. was supported by NIH Grant T32 GM108563.
  • Added Creator WILLIAM O HANCOCK
  • Added 20250430_Source_Data.xlsx
  • Added Readme.txt
  • Updated
  • Updated Publication Date Show Changes
    Publication Date
    • 2025
    • 2025-05-05
  • Added Creator RUI JIANG
  • Updated License Show Changes
    License
    • https://creativecommons.org/licenses/by-nc/4.0/
  • Published
  • Updated
  • Updated Publisher, Related URLs Show Changes
    Publisher
    • Biophysical Journal
    Related URLs
    • https://doi.org/10.1016/j.bpj.2025.04.033, https://doi.org/10.1101/2024.10.23.619892
  • Renamed Creator William O. Hancock Show Changes
    • WILLIAM O HANCOCK
    • William O. Hancock
  • Renamed Creator Rui Jiang Show Changes
    • RUI JIANG
    • Rui Jiang