Evidence map›Paper›PMID 29604873›Full record

ArticleThe Journal of chemical physics2018

A fluid membrane enhances the velocity of cargo transport by small teams of kinesin-1.

Qiaochu Li, Kuo-Fu Tseng, Stephen J King, Weihong Qiu, Jing Xu

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. ADP release can explain spatially-dependent kinesin binding times.bioRxiv : the preprint server for biology · 2023
    Article
  7. Logistics of Bone Mineralization in the Chick Embryo Studied by 3D Cryo FIB-SEM Imaging.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  8. 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 · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Qiaochu LiDepartment of Physics, University of California, Merced, California 95343, USA.
Kuo-Fu TsengDepartment of Physics, Oregon State University, Corvallis, Oregon 97331, USA.
Stephen J KingBurnett School of Biomedical Sciences, University of Central Florida, Orlando, Florida 32827, USA.
Weihong QiuDepartment of Physics, Oregon State University, Corvallis, Oregon 97331, USA.ORCID 0000000314131389
Jing XuDepartment of Physics, University of California, Merced, California 95343, USA.ORCID 0000000278829105

Funding

Dynactin/microtubule interactions in dynein motilityR01NS048501 · NINDS · UNIVERSITY OF MISSOURI KANSAS CITY · PI KING, STEPHEN J · 2004 to 2014
$2.9M
Do Cargo Membrane Fluidity and Microdomain Formation Impact Motor Protein-Based Motility?R15GM120682 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI XU, JING · 2016 to 2024
$1.4M
NIGMS NIH HHS R15 GM120682NINDS NIH HHS R01 NS048501
6 · The paper itself

Abstract

Kinesin-1 (hereafter referred to as kinesin) is a major microtubule-based motor protein for plus-end-directed intracellular transport in live cells. While the single-molecule functions of kinesin are well characterized, the physiologically relevant transport of membranous cargos by small teams of kinesins remains poorly understood. A key experimental challenge remains in the quantitative control of the number of motors driving transport. Here we utilized "motile fraction" to overcome this challenge and experimentally accessed transport by a single kinesin through the physiologically relevant transport by a small team of kinesins. We used a fluid lipid bilayer to model the cellular membrane in vitro and employed optical trapping to quantify the transport of membrane-enclosed cargos versus traditional membrane-free cargos under identical conditions. We found that coupling motors via a fluid membrane significantly enhances the velocity of cargo transport by small teams of kinesins. Importantly, enclosing a cargo in a fluid lipid membrane did not impact single-kinesin transport, indicating that membrane-dependent velocity enhancement for team-based transport arises from altered interactions between kinesins. Our study demonstrates that membrane-based coupling between motors is a key determinant of kinesin-based transport. Enhanced velocity may be critical for fast delivery of cargos in live cells.

Indexed as

Models, BiologicalBiological TransportHydrodynamicsKinesinsMembranesKinesins

Identifiers

PMID29604873
PMCPMC6910576

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.