Evidence map›Paper›PMID 11018061›Full record

ArticleThe Journal of cell biology2000

Dynein, dynactin, and kinesin II's interaction with microtubules is regulated during bidirectional organelle transport.

E L Reese, L T Haimo

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Dynactin polices two-way organelle traffic.The Journal of cell biology · 2003
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Insulin can regulate GLUT4 internalization by signaling to Rab5 and the motor protein dynein.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  9. Article
  10. Self-organization of a radial microtubule array by dynein-dependent nucleation of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  11. Article
  12. Sorting and directed transport of membrane proteins during development of hippocampal neurons in culture.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  13. Article
  14. Article
  15. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

E L ReeseDepartment of Biology, University of California at Riverside, Riverside, California 92521, USA.
L T Haimo
University of California, Riverside · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The microtubule motors, cytoplasmic dynein and kinesin II, drive pigmented organelles in opposite directions in Xenopus melanophores, but the mechanism by which these or other motors are regulated to control the direction of organelle transport has not been previously elucidated. We find that cytoplasmic dynein, dynactin, and kinesin II remain on pigment granules during aggregation and dispersion in melanophores, indicating that control of direction is not mediated by a cyclic association of motors with these organelles. However, the ability of dynein, dynactin, and kinesin II to bind to microtubules varies as a function of the state of aggregation or dispersion of the pigment in the cells from which these molecules are isolated. Dynein and dynactin bind to microtubules when obtained from cells with aggregated pigment, whereas kinesin II binds to microtubules when obtained from cells with dispersed pigment. Moreover, the microtubule binding activity of these motors/dynactin can be reversed in vitro by the kinases and phosphatase that regulate the direction of pigment granule transport in vivo. These findings suggest that phosphorylation controls the direction of pigment granule transport by altering the ability of dynein, dynactin, and kinesin II to interact with microtubules.

Indexed as

AnimalsBiological TransportCalcium-Binding ProteinsCell LineCyclic AMP-Dependent Protein KinasesCytoplasmic GranulesDynactin ComplexDyneinsKinesinsMelanophoresMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalMolecular Motor ProteinsMovementMuscle ProteinsCalcium-Binding ProteinsCyclic AMP-Dependent Protein KinasesDynactin ComplexDyneinskinesin-IIKinesinsMicrotubule-Associated ProteinsMolecular Motor ProteinsMuscle ProteinsPhosphoprotein PhosphatasesPigments, BiologicalProtein Kinase CXenopus ProteinsXKLP3 protein, Xenopus

Identifiers

PMID11018061
PMCPMC2189799
OpenAlexW2055744054

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.