Evidence map›Paper›PMID 11827982›Full record

ArticleThe Journal of cell biology2002

The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p.

Andrea R Castillo, Janet B Meehl, Garry Morgan, Amy Schutz-Geschwender, Mark Winey

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. The MPS1 family of protein kinases.Annual review of biochemistry · 2012
    Review
  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 at 2 institutions in 1 country.

Andrea R CastilloMCD Biology, UCB 347, University of Colorado, Boulder CO 80309, USA.
Janet B Meehl
Garry Morgan
Amy Schutz-Geschwender
Mark Winey
University of Colorado Boulder · USLI-COR Biosciences (United States) · US

Funding

Role of MPSI Kinase and Yeast Spindle Pole CycleR01GM051312 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI WINEY, MARK · 1994 to 2015
$5.1M
MPSL KINASE AND YEAST SPINDLE POLE BODY CYCLEF31GM019566 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CASTILLO, ANDREA R · 1998 to 1999
–
NIGMS NIH HHS F31 GM019566NIGMS NIH HHS GM19566NIGMS NIH HHS GM51312NIGMS NIH HHS R01 GM051312
6 · The paper itself

Abstract

Saccharomyces cerevisiae MPS1 encodes an essential protein kinase that has roles in spindle pole body (SPB) duplication and the spindle checkpoint. Previously characterized MPS1 mutants fail in both functions, leading to aberrant DNA segregation with lethal consequences. Here, we report the identification of a unique conditional allele, mps1-8, that is defective in SPB duplication but not the spindle checkpoint. The mutations in mps1-8 are in the noncatalytic region of MPS1, and analysis of the mutant protein indicates that Mps1-8p has wild-type kinase activity in vitro. A screen for dosage suppressors of the mps1-8 conditional growth phenotype identified the gene encoding the integral SPB component SPC42. Additional analysis revealed that mps1-8 exhibits synthetic growth defects when combined with certain mutant alleles of SPC42. An epitope-tagged version of Mps1p (Mps1p-myc) localizes to SPBs and kinetochores by immunofluorescence microscopy and immuno-EM analysis. This is consistent with the physical interaction we detect between Mps1p and Spc42p by coimmunoprecipitation. Spc42p is a substrate for Mps1p phosphorylation in vitro, and Spc42p phosphorylation is dependent on Mps1p in vivo. Finally, Spc42p assembly is abnormal in a mps1-1 mutant strain. We conclude that Mps1p regulates assembly of the integral SPB component Spc42p during SPB duplication.

Indexed as

Saccharomyces cerevisiae ProteinsAllelesAmino Acid SequenceCentrosomeCytoskeletal ProteinsFluorescent Antibody TechniqueGene DosageGenes, cdcKinetochoresMicroscopy, ElectronMitosisMutationPhosphoproteinsPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryCytoskeletal ProteinsMPS1 protein, S cerevisiaePhosphoproteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesSaccharomyces cerevisiae ProteinsSPC42 protein, S cerevisiae

Identifiers

PMID11827982
PMCPMC2173341
OpenAlexW2003550324

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.