Evidence map›Paper›PMID 9660870›Full record

ArticleThe Journal of cell biology1998

Functional specialization of stable and dynamic microtubules in protein traffic in WIF-B cells.

C Poüs, K Chabin, A Drechou, L Barbot, T Phung-Koskas, C Settegrana, M L Bourguet-Kondracki, M Maurice, D Cassio, M Guyot and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Hepatocyte polarity.Comprehensive Physiology · 2013
    Review
  7. Article
  8. Article
  9. Alcohol-induced alterations of the hepatocyte cytoskeleton.World journal of gastroenterology · 2010
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

11 authors at 3 institutions in 1 country.

C PoüsLaboratoire de Biochimie Générale, Equipe d'Accueil 1595, Unité de Formation et de Recherche de Pharmacie, Université Paris-Sud, 92296 Châtenay-Malabry, France.
K Chabin
A Drechou
L Barbot
T Phung-Koskas
C Settegrana
M L Bourguet-Kondracki
M Maurice
D Cassio
M Guyot
G Durand
Institut Curie · FRUniversité Paris Cité · FRUniversité Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We found that the magnesium salt of ilimaquinone, named 201-F, specifically disassembled dynamically unstable microtubules in fibroblasts and various epithelial cell lines. Unlike classical tubulin- interacting drugs such as nocodazole or colchicine which affect all classes of microtubules, 201-F did not depolymerize stable microtubules. In WIF-B-polarized hepatic cells, 201-F disrupted the Golgi complex and inhibited albumin and alpha1-antitrypsin secretion to the same extent as nocodazole. By contrast, 201-F did not impair the transport of membrane proteins to the basolateral surface, which was only affected by the total disassembly of cellular microtubules. Transcytosis of two apical membrane proteins-the alkaline phosphodiesterase B10 and dipeptidyl peptidase IV-was affected to the same extent by 201-F and nocodazole. Taken together, these results indicate that only dynamically unstable microtubules are involved in the transport of secretory proteins to the plasma membrane, and in the transcytosis of membrane proteins to the apical surface. By contrast, stable microtubules, which are not functionally affected by 201-F treatment, are involved in the transport of membrane proteins to the basolateral surface. By specifically disassembling highly dynamic microtubules, 201-F is an invaluable tool with which to study the functional specialization of stable and dynamic microtubules in living cells.

Indexed as

Albuminsalpha 1-AntitrypsinAnimalsBiological TransportCell LineDogsHeLa CellsHumansMicrotubulesNocodazolePhosphodiesterase IPhosphoric Diester HydrolasesProteinsQuinonesAlbuminsalpha 1-AntitrypsinillimaquinoneNocodazolePhosphodiesterase IPhosphoric Diester HydrolasesProteinsQuinones

Identifiers

PMID9660870
PMCPMC2133029
OpenAlexW2152335956

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.