Evidence map›Paper›PMID 14565986›Full record

ArticleMolecular biology of the cell2003

Analysis of the dynein-dynactin interaction in vitro and in vivo.

Stephen J King, Christa L Brown, Kerstin C Maier, Nicholas J Quintyne, Trina A Schroer

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

109 citing papers in PubMed, 180 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Article
  8. MINFLUX reveals dynein stepping in live neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Dynactin 1 negatively regulates HIV-1 infection by sequestering the host cofactor CLIP170.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article

49 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

5 authors at 1 institution in 1 country.

Stephen J KingDepartment of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
Christa L Brown
Kerstin C Maier
Nicholas J Quintyne
Trina A Schroer
Johns Hopkins University · US

Funding

REGULATION OF CYTOPLASMIC DYNEIN-BASED VESICLE TRANSPORTR01GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 1990 to 2012
$4.3M
TARGETING OF MEMBRANE PROTEINS IN POLARIZED EPITHELIAP01DK044375 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI HUBBARD, ANN L · 1992 to 2002
$3.0M
Regulation of Cytoplasmic Dynein Based Vesicle TransportR56GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 2008 to 2008
$410k
NIDDK NIH HHS DK-44375NIGMS NIH HHS GM-44589NIGMS NIH HHS R01 GM044589NIGMS NIH HHS R56 GM044589
6 · The paper itself

Abstract

Cytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context. Solution binding assays were used to define binding domains in the dynein intermediate chain (IC) and dynactin p150Glued subunit. Transient overexpression of a series of fragments of the dynein IC was used to determine the importance of this subunit for dynein function in mammalian tissue culture cells. Our results suggest that a functional dynein-dynactin interaction is required for proper microtubule organization and for the transport and localization of centrosomal components and endomembrane compartments. The dynein IC fragments have different effects on endomembrane localization, suggesting that different endomembranes may bind dynein via distinct mechanisms.

Indexed as

AnimalsCell CompartmentationChlorocebus aethiopsCOS CellsDynactin ComplexDyneinsEndocytosisEndosomesGreen Fluorescent ProteinsHeLa CellsHumansLuminescent ProteinsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesProtein BindingDynactin ComplexDyneinsGreen Fluorescent ProteinsLuminescent ProteinsMicrotubule-Associated ProteinsProtein Subunits

Identifiers

PMID14565986
PMCPMC284810
OpenAlexW2145723402

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.