Evidence map›Paper›PMID 21633107›Full record

ArticleMolecular biology of the cell2011

Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning.

Melissa D Stuchell-Brereton, Amanda Siglin, Jun Li, Jeffrey K Moore, Shubbir Ahmed, John C Williams, John A Cooper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Optimization of Sperm Cryopreservation Formulation inInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. eLife · 2017
    Article
  11. TheJournal of cell science · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Stopped in its tracks: negative regulation of the dynein motor by the yeast protein She1.BioEssays : news and reviews in molecular, cellular and developmental biology · 2013
    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

7 authors at 3 institutions in 1 country.

Melissa D Stuchell-BreretonDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Amanda Siglin
Jun Li
Jeffrey K Moore
Shubbir Ahmed
John C Williams
John A Cooper
Washington University in St. Louis · USThomas Jefferson University · USCity of Hope · US

Funding

MOLECULAR ONCOLOGY TRAINING GRANTT32CA113275 · NCI · WASHINGTON UNIVERSITY · PI Matthew J Walter · 2006 to 2026
$5.7M
The Function of Dynein in Budding YeastR01GM047337 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1993 to 2009
$2.6M
Analytical UltracentrifugeS10RR022316 · NCRR · THOMAS JEFFERSON UNIVERSITY · PI WILLIAMS, JOHN CHARLES · 2007 to 2007
$284k
NCI NIH HHS T-32-CA113275NCI NIH HHS T32 CA113275NCRR NIH HHS RR022316-01A1NCRR NIH HHS S10 RR022316NIGMS NIH HHS GM47337NIGMS NIH HHS R01 GM047337
6 · The paper itself

Abstract

Cytoplasmic dynein is a large multisubunit complex involved in retrograde transport and the positioning of various organelles. Dynein light chain (LC) subunits are conserved across species; however, the molecular contribution of LCs to dynein function remains controversial. One model suggests that LCs act as cargo-binding scaffolds. Alternatively, LCs are proposed to stabilize the intermediate chains (ICs) of the dynein complex. To examine the role of LCs in dynein function, we used Saccharomyces cerevisiae, in which the sole function of dynein is to position the spindle during mitosis. We report that the LC8 homologue, Dyn2, localizes with the dynein complex at microtubule ends and interacts directly with the yeast IC, Pac11. We identify two Dyn2-binding sites in Pac11 that exert differential effects on Dyn2-binding and dynein function. Mutations disrupting Dyn2 elicit a partial loss-of-dynein phenotype and impair the recruitment of the dynein activator complex, dynactin. Together these results indicate that the dynein-based function of Dyn2 is via its interaction with the dynein IC and that this interaction is important for the interaction of dynein and dynactin. In addition, these data provide the first direct evidence that LC occupancy in the dynein motor complex is important for function.

Indexed as

Signal TransductionAmino Acid SequenceBinding SitesCloning, MolecularDynactin ComplexDyneinsEscherichia coliMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesMitosisMolecular Sequence DataMutationPlasmidsProtein BindingRecombinant ProteinsDynactin ComplexDyneinsintermediate chain 1 protein, S cerevisiaeMicrotubule-Associated ProteinsRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21633107
PMCPMC3145545
OpenAlexW2122401596

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.