Evidence map›Paper›PMID 8636213›Full record

ArticleThe Journal of cell biology1996

Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level.

X M Wang, J G Peloquin, Y Zhai, J C Bulinski, G G Borisy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Regulation of microtubule-based transport by MAP4.Molecular biology of the cell · 2014
    Article
  3. The role of microtubules and their dynamics in cell migration.The Journal of biological chemistry · 2012
    Article
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  5. Review
  6. Article
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  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Acute inactivation of tau has no effect on dynamics of microtubules in growing axons of cultured sympathetic neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  17. Nonneuronal isoforms of STOP protein are responsible for microtubule cold stability in mammalian fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

X M WangLaboratory of Molecular Biology, University of Wisconsin-Madison 53706, USA.
J G Peloquin
Y Zhai
J C Bulinski
G G Borisy
University of Wisconsin–Madison · US

Funding

MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLYR01GM025062 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BORISY, GARY G · 1985 to 2003
$1.9M
MECHANISM AND CONTROL OF MICROTUBULE ASSEMBLYR37GM025062 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI BORISY, GARY G · 1989 to 1998
–
NIGMS NIH HHS GM 25062
6 · The paper itself

Abstract

Microtubule-associated protein 4 (MAP4) promotes MT assembly in vitro and is localized along MTs in vivo. These results and the fact that MAP4 is the major MAP in nonneuronal cells suggest that MAP4's normal functions may include the stabilization of MTs in situ. To understand MAP4 function in vivo, we produced a blocking antibody (Ab) to prevent MAP4 binding to MTs. The COOH-terminal MT binding domain of MAP4 was expressed in Escherichia coli as a glutathione transferase fusion protein and was injected into rabbits to produce an antiserum that was then affinity purified and shown to be monospecific for MAP4. This Ab blocked > 95% of MAP4 binding to MTs in an in vitro assay. Microinjection of the affinity purified Ab into human fibroblasts and monkey epithelial cells abolished MAP4 binding to MTs as assayed with a rat polyclonal antibody against the NH2-terminal projection domain of MAP4. The removal of MAP4 from MTs was accompanied by its sequestration into visible MAP4-Ab immunocomplexes. However, the MT network appeared normal. Tubulin photoactivation and nocodazole sensitivity assays indicated that MT dynamics were not altered detectably by the removal of MAP4 from the MTs. Cells progressed to mitosis with morphologically normal spindles in the absence of MAP4 binding to MTs. Depleting MAP4 from MTs also did not affect the state of posttranslational modifications of tubulin subunits. Further, no perturbations of MT-dependent organelle distribution were detected. We conclude that the association of MAP4 with MTs is not essential for MT assembly or for the MT-based functions in cultured cells that we could assay. A significant role for MAP4 is not excluded by these results, however, as MAP4 may be a component of a functionally redundant system.

Indexed as

AnimalsAntibody SpecificityBrainCell LineCells, CulturedCloning, MolecularEscherichia coliFibroblastsGlutathione TransferaseGolgi ApparatusHaplorhiniHeLa CellsHumansImmune SeraMaleMicrotubule-Associated ProteinsGlutathione TransferaseImmune SeraMicrotubule-Associated ProteinsNocodazoleRecombinant Fusion ProteinsTubulin

Identifiers

PMID8636213
PMCPMC2120719
OpenAlexW2155369749

What OpenQuestion holds

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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.