Evidence map›Paper›PMID 19293377›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Regulation of the processivity and intracellular localization of Saccharomyces cerevisiae dynein by dynactin.

Julia R Kardon, Samara L Reck-Peterson, Ronald D Vale

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

84 citing papers in PubMed, 139 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021
    Review
  7. Article
  8. Article
  9. Activation and Regulation of Cytoplasmic Dynein.Trends in biochemical sciences · 2020
    Review
  10. Article
  11. Article
  12. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. TheJournal of cell science · 2017
    Article
  18. Article
  19. Article
  20. Review

24 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 2 institutions in 1 country.

Julia R KardonDepartment of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA.
Samara L Reck-Peterson
Ronald D Vale
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

STRUCTURE/FUNCTION OF MOLECULAR MOTORSP01AR042895 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COOKE, ROGER A · 1994 to 2008
$9.8M
Structure and mechanism of the dynein motorR01GM097312 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2011 to 2016
$1.5M
Howard Hughes Medical InstituteNIAMS NIH HHS P01 AR042895NIAMS NIH HHS P01-AR42895NIGMS NIH HHS R01 GM097312
6 · The paper itself

Abstract

Dynactin, a large multisubunit complex, is required for intracellular transport by dynein; however, its cellular functions and mechanism of action are not clear. Prior studies suggested that dynactin increases dynein processivity by tethering the motor to the microtubule through its own microtubule binding domains. However, this hypothesis could not be tested without a recombinant source of dynactin. Here, we have produced recombinant dynactin and dynein in Saccharomyces cerevisiae, and examined the effect of dynactin on dynein in single-molecule motility assays. We show that dynactin increases the run length of single dynein motors, but does not alter the directionality of dynein movement. Enhancement of dynein processivity by dynactin does not require the microtubule (MT) binding domains of Nip100 (the yeast p150(Glued) homolog). Dynactin lacking these MT binding domains also supports the proper localization and function of dynein during nuclear segregation in vivo. Instead, a segment of the coiled-coil of Nip100 is required for these activities. Our results directly demonstrate that dynactin increases the processivity of dynein through a mechanism independent of microtubule tethering.

Indexed as

Dynactin ComplexDyneinsMicrotubule-Associated ProteinsMicrotubulesMolecular Motor ProteinsMotionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDynactin ComplexDyneinsMicrotubule-Associated ProteinsMolecular Motor ProteinsNIP100 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19293377
PMCPMC2657088
OpenAlexW1974276027

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.