Evidence map›Paper›PMID 8816999›Full record

ArticleMolecular biology of the cell1996

Overexpression of cytoplasmic dynein's globular head causes a collapse of the interphase microtubule network in Dictyostelium.

M P Koonce, M Samsó

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
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

33 citing papers in PubMed.

  1. Article
  2. TheCells · 2021
    Review
  3. Review
  4. Methods and protocols · 2020
    Article
  5. Bioenergetics of theBiomolecules · 2020
    Article
  6. Review
  7. Review
  8. Article
  9. Mechanism and regulation of cytoplasmic dynein.Annual review of cell and developmental biology · 2015
    Review
  10. Functions and mechanics of dynein motor proteins.Nature reviews. Molecular cell biology · 2013
    Review
  11. A kinesin-mediated mechanism that couples centrosomes to nuclei.Cellular and molecular life sciences : CMLS · 2013
    Article
  12. Article
  13. X-ray structure of a functional full-length dynein motor domain.Nature structural & molecular biology · 2011
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  19. Two modes of microtubule sliding driven by cytoplasmic dynein.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

2 authors.

M P KoonceDivision of Molecular Medicine, Wadsworth Center, Albany, New York 12201-0509, USA.
M Samsó

Funding

STRUCTURE ANALYSIS OF MACROMOLECULAR ASSEMBLIESR01GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1985 to 2019
$6.1M
STRUCTURAL ANALYSIS OF MACROMOLECULAR ASSEMBLYR37GM029169 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2006
$2.8M
MOLECULAR CHARACTERIZATION OF A CYTOPLASMIC DYNEINR01GM051532 · NIGMS · WADSWORTH CENTER · PI KOONCE, MICHAEL P · 2001 to 2004
$1.0M
MOLECULAR CHARACTERIZATION OF A CYTOPLASMIC DYNEINR29GM051532 · NIGMS · WADSWORTH CENTER · PI KOONCE, MICHAEL P · 1994 to 1998
–
NIGMS NIH HHS GM-29169NIGMS NIH HHS GM-51532
6 · The paper itself

Abstract

Cytoplasmic dynein is a minus-end directed microtubule-based motor. Using a molecular genetic approach, we have begun to dissect structure-function relationships of dynein in the cellular slime mold Dictyostelium. Expression of a carboxy-terminal 380-kDa fragment of the heavy chain produces a protein that approximates the size and shape of the globular, mechanochemical head of dynein. This polypeptide cosediments with microtubules in an ATP-sensitive fashion and undergoes a UV-vanadate cleavage reaction. The deleted amino-terminal region appears to participate in dimerization of the native protein and in binding the intermediate and light chains. Overexpression of the 380-kDa carboxy-terminal construct in Dictyostelium produces a distinct phenotype in which the interphase radial microtubule array appears collapsed. In many cells, the microtubules form loose bundles that are whorled around the nucleus. Similar expression of a central 107-kDa fragment of the heavy chain does not produce this result. The data presented here suggest that dynein may participate in maintaining the spatial pattern of the interphase microtubule network.

Indexed as

AnimalsCytoplasmCytoskeletonDictyosteliumDyneinsInterphaseMicroscopy, ElectronMicrotubulesMolecular StructurePhenotypeStructure-Activity RelationshipDyneins

Identifiers

PMID8816999
PMCPMC275944

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.