Evidence map›Paper›PMID 1387874›Full record

ArticleThe Journal of cell biology1992

Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex.

I Corthésy-Theulaz, A Pauloin, S R Pfeffer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

112 citing papers in PubMed, 283 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  6. Article
  7. Article
  8. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
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  18. Review
  19. Article
  20. Review

52 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

3 authors at 1 institution in 1 country.

I Corthésy-TheulazDepartment of Biochemistry, Stanford University School of Medicine 94305-5307.
A Pauloin
S R Pfeffer
Stanford University · US

Funding

INTRACELLULAR TRANSPORT--THE MANNOSE/PHOSPHATE RECEPTORR01DK037332 · NIDDK · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 1986 to 2019
$4.7M
INTRACELLULAR TRANSPORT--THE MANNOSE-PHOSPHATE RECEPTORR37DK037332 · NIDDK · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 1999 to 2008
$3.4M
Intracellular Transport-The Mannose Phosphate ReceptorR56DK037332 · NIDDK · STANFORD UNIVERSITY · PI PFEFFER, SUZANNE R · 2014 to 2014
$120k
NIDDK NIH HHS DK-37332
6 · The paper itself

Abstract

The localization of the Golgi complex depends upon the integrity of the microtubule apparatus. At interphase, the Golgi has a restricted pericentriolar localization. During mitosis, it fragments into small vesicles that are dispersed throughout the cytoplasm until telophase, when they again coalesce near the centrosome. These observations have suggested that the Golgi complex utilizes a dynein-like motor to mediate its transport from the cell periphery towards the minus ends of microtubules, located at the centrosome. We utilized semi-intact cells to study the interaction of the Golgi complex with the microtubule apparatus. We show here that Golgi complexes can enter semi-intact cells and associate stably with cytoplasmic constituents. Stable association, termed here "Golgi capture," requires ATP hydrolysis and intact microtubules, and occurs maximally at physiological temperature in the presence of added cytosolic proteins. Once translocated into the semi-intact cell cytoplasm, exogenous Golgi complexes display a distribution similar to endogenous Golgi complexes, near the microtubule-organizing center. The process of Golgi capture requires cytoplasmic tubulin, and is abolished if cytoplasmic dynein is immunodepleted from the cytosol. Cytoplasmic dynein, prepared from CHO cell cytosol, restores Golgi capture activity to reactions carried out with dynein immuno-depleted cytosol. These results indicate that cytoplasmic dynein can interact with isolated Golgi complexes, and participate in their accumulation near the centrosomes of semi-intact, recipient cells. Thus, cytoplasmic dynein appears to play a role in determining the subcellular localization of the Golgi complex.

Indexed as

Adenosine TriphosphateAnimalsCHO CellsCricetinaeCytoplasmDyneinsFluorescent Antibody TechniqueGolgi ApparatusMicrotubulesAdenosine TriphosphateDyneins

Identifiers

PMID1387874
PMCPMC2289611
OpenAlexW2011730020

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.