Evidence map›Paper›PMID 12058056›Full record

ArticleMolecular biology of the cell2002

Stu1p is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle.

Hongwei Yin, Liru You, Danielle Pasqualone, Kristen M Kopski, Tim C Huffaker

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. TheCells · 2025
    Article
  5. Article
  6. MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. CLASPs at a glance.Journal of cell science · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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.

Hongwei YinDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703, USA.
Liru You
Danielle Pasqualone
Kristen M Kopski
Tim C Huffaker

Funding

MOLECULAR ANALYSIS OF MICROTUBULE FUNCTION IN YEASTR01GM040479 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HUFFAKER, TIM C · 1988 to 2010
$2.6M
NIGMS NIH HHS GM-40479NIGMS NIH HHS R01 GM040479
6 · The paper itself

Abstract

Formation of the bipolar mitotic spindle relies on a balance of forces acting on the spindle poles. The primary outward force is generated by the kinesin-related proteins of the BimC family that cross-link antiparallel interpolar microtubules and slide them past each other. Here, we provide evidence that Stu1p is also required for the production of this outward force in the yeast Saccharomyces cerevisiae. In the temperature-sensitive stu1-5 mutant, spindle pole separation is inhibited, and preanaphase spindles collapse, with their previously separated poles being drawn together. The temperature sensitivity of stu1-5 can be suppressed by doubling the dosage of Cin8p, a yeast BimC kinesin-related protein. Stu1p was observed to be a component of the mitotic spindle localizing to the midregion of anaphase spindles. It also binds to microtubules in vitro, and we have examined the nature of this interaction. We show that Stu1p interacts specifically with beta-tubulin and identify the domains required for this interaction on both Stu1p and beta-tubulin. Taken together, these findings suggest that Stu1p binds to interpolar microtubules of the mitotic spindle and plays an essential role in their ability to provide an outward force on the spindle poles.

Indexed as

Base SequenceDNA PrimersGenotypeMicrotubule-Associated ProteinsModels, MolecularMutagenesisProtein BiosynthesisProtein ConformationRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusTranscription, GeneticTubulinDNA PrimersMicrotubule-Associated ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSTU1 protein, S cerevisiaeTubulin

Identifiers

PMID12058056
PMCPMC117611

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.