Evidence map›Paper›PMID 3141429›Full record

ArticleThe Journal of cell biology1988

The role of kinesin and other soluble factors in organelle movement along microtubules.

T A Schroer, B J Schnapp, T S Reese, M P Sheetz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
8.8field-weighted citation impact, top 2% of its field
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

53 citing papers in PubMed, 178 citations in OpenAlex.

  1. Review
  2. AMPK Preferentially Depresses Retrograde Transport of Axonal Mitochondria during Localized Nutrient Deprivation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
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  13. No conventional function for the conventional kinesin?Traffic (Copenhagen, Denmark) · 2008
    Article
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  20. PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

4 authors at 1 institution in 1 country.

T A SchroerDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
B J Schnapp
T S Reese
M P Sheetz
Washington University in St. Louis · US

Funding

STRUCTURE AND ASSEMBLY OF CYTOSKELETAL FILAMENTSR01GM036277 · NIGMS · WASHINGTON UNIVERSITY · PI SHEETZ, MICHAEL PATRICK · 1985 to 2009
$2.8M
NIGMS NIH HHS GM36277NINDS NIH HHS NS2345
6 · The paper itself

Abstract

Kinesin is a force-generating ATPase that drives the sliding movement of microtubules on glass coverslips and the movement of plastic beads along microtubules. Although kinesin is suspected to participate in microtubule-based organelle transport, the exact role it plays in this process is unclear. To address this question, we have developed a quantitative assay that allows us to determine the ability of soluble factors to promote organelle movement. Salt-washed organelles from squid axoplasm exhibited a nearly undetectable level of movement on purified microtubules. Their frequency of movement could be increased greater than 20-fold by the addition of a high speed axoplasmic supernatant. Immunoadsorption of kinesin from this supernatant decreased the frequency of organelle movement by more than 70%; organelle movements in both directions were markedly reduced. Surprisingly, antibody purified kinesin did not promote organelle movement either by itself or when it was added back to the kinesin-depleted supernatant. This result suggested that other soluble factors necessary for organelle movement were removed along with kinesin during immunoadsorption of the supernatant. A high level of organelle motor activity was recovered in a high salt eluate of the immunoadsorbent that contained only little kinesin. On the basis of these results we propose that organelle movement on microtubules involves other soluble axoplasmic factors in addition to kinesin.

Indexed as

AnimalsAntibodies, MonoclonalAxonsBiological FactorsBiological TransportDecapodiformesDensitometryIn Vitro TechniquesKinesinsMicrotubulesModels, BiologicalNerve Tissue ProteinsOrganellesPotassium IodideSolubilityAntibodies, MonoclonalBiological FactorsKinesinsNerve Tissue ProteinsPotassium Iodide

Identifiers

PMID3141429
PMCPMC2115347
OpenAlexW2133771191

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.