Evidence map›Paper›PMID 9105041›Full record

ArticleThe Journal of cell biology1997

Molecular requirements for bi-directional movement of phagosomes along microtubules.

A Blocker, F F Severin, J K Burkhardt, J B Bingham, H Yu, J C Olivo, T A Schroer, A A Hyman, G Griffiths

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.1field-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

78 citing papers in PubMed, 232 citations in OpenAlex.

  1. Article
  2. Article
  3. Phagocytosis at a glance.Journal of cell science · 2025
    Review
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  7. Article
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  10. Article
  11. Article
  12. Review
  13. Motor Proteins and Spermatogenesis.Advances in experimental medicine and biology · 2021
    Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

18 more citing papers are in PubMed but not listed here.

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

9 authors at 2 institutions in 2 countries.

A BlockerCell Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany. ablocker@pasteur.fr
F F Severin
J K Burkhardt
J B Bingham
H Yu
J C Olivo
T A Schroer
A A Hyman
G Griffiths
Johns Hopkins University · USEuropean Molecular Biology Laboratory · DE

Funding

REGULATION OF CYTOPLASMIC DYNEIN-BASED VESICLE TRANSPORTR01GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 1990 to 2012
$4.3M
NIGMS NIH HHS R01 GM044589
6 · The paper itself

Abstract

Microtubules facilitate the maturation of phagosomes by favoring their interactions with endocytic compartments. Here, we show that phagosomes move within cells along tracks of several microns centrifugally and centripetally in a pH- and microtubule-dependent manner. Phagosome movement was reconstituted in vitro and required energy, cytosol and membrane proteins of this organelle. The activity or presence of these phagosome proteins was regulated as the organelle matured, with "late" phagosomes moving threefold more frequently than "early" ones. The majority of moving phagosomes were minus-end directed; the remainder moved towards microtubule plus-ends and a small subset moved bi-directionally. Minus-end movement showed pharmacological characteristics expected for dyneins, was inhibited by immunodepletion of cytoplasmic dynein and could be restored by addition of cytoplasmic dynein. Plus-end movement displayed pharmacological properties of kinesin, was inhibited partially by immunodepletion of kinesin and fully by addition of an anti-kinesin IgG. Immunodepletion of dynactin, a dynein-activating complex, inhibited only minus-end directed motility. Evidence is provided for a dynactin-associated kinase required for dynein-mediated vesicle transport. Movement in both directions was inhibited by peptide fragments from kinectin (a putative kinesin membrane receptor), derived from the region to which a motility-blocking antibody binds. Polypeptide subunits from these microtubule-based motility factors were detected on phagosomes by immunoblotting or immunoelectron microscopy. This is the first study using a single in vitro system that describes the roles played by kinesin, kinectin, cytoplasmic dynein, and dynactin in the microtubule-mediated movement of a purified membrane organelle.

Indexed as

Adenosine TriphosphateAnimalsBiological TransportCells, CulturedCytosolDynactin ComplexDyneinsHydrogen-Ion ConcentrationKidneyKinesinsLatexMacrophagesMembrane ProteinsMiceMicrospheresMicrotubule-Associated ProteinsAdenosine TriphosphateDynactin ComplexDyneinsKinesinsKTN1 protein, humanKtn1 protein, mouseLatexMembrane ProteinsMicrotubule-Associated ProteinsPhosphotransferasesReceptors, Cell Surface

Identifiers

PMID9105041
PMCPMC2139871
OpenAlexW2165991313

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.