Evidence map›Paper›PMID 17198398›Full record

ArticleBiochemistry2007

Arg-Pro-X-Ser/Thr is a consensus phosphoacceptor sequence for the meiosis-specific Ime2 protein kinase in Saccharomyces cerevisiae.

Michael Moore, Marcus E Shin, Adrian Bruning, Karen Schindler, Andrew Vershon, Edward Winter

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024
    Review
  3. Article
  4. Phospho-Regulation of Meiotic Prophase.Frontiers in cell and developmental biology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Sic1-induced DNA rereplication during meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

6 authors at 2 institutions in 1 country.

Michael MooreDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Marcus E Shin
Adrian Bruning
Karen Schindler
Andrew Vershon
Edward Winter
Rutgers, The State University of New Jersey · USThomas Jefferson University · US

Funding

TRAINING PROGRAM IN BIOMOLECULAR SIGNAL TRANSDUCTIONT32DK007705 · NIDDK · THOMAS JEFFERSON UNIVERSITY · PI BENOVIC, JEFFREY L · 1994 to 2008
$2.6M
THE SMKI MAPK AND SPORE DEVELOPMENT IN SACCHAROMYCESR01GM061817 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI WINTER, EDWARD P · 2000 to 2010
$2.1M
TRANSCRIPTIONAL REGULATION OF MEIOTIC GENES IN YEASTR01GM058762 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI VERSHON, ANDREW · 2000 to 2003
$799k
NIDDK NIH HHS T32-DK07705NIGMS NIH HHS GM 061817NIGMS NIH HHS GM 58762NIGMS NIH HHS R01 GM058762NIGMS NIH HHS R01 GM061817
6 · The paper itself

Abstract

Ime2 is a meiosis-specific protein kinase in Saccharomyces cerevisiae that is functionally related to cyclin-dependent kinase. Although Ime2 regulates multiple steps in meiosis, only a few of its substrates have been identified. Here we show that Ime2 phosphorylates Sum1, a repressor of meiotic gene transcription, on Thr-306. Ime2 protein kinase assays with Sum1 mutants and synthetic peptides define a consensus Arg-Pro-X-Ser/Thr motif that is required for efficient phosphorylation by Ime2. The carboxyl residue adjacent to the phosphoacceptor (+1 position) also influences the efficiency of Ime2 phosphorylation with alanine being a preferred residue. This information has predictive value in identifying new potential Ime2 targets as shown by the ability of Ime2 to phosphorylate Sgs1 and Gip1 in vitro and could be important in differentiating mitotic and meiotic regulatory pathways.

Indexed as

MeiosisAmino Acid MotifsCarrier ProteinsCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsPhosphorylationProtein KinasesProtein Phosphatase 1Protein Serine-Threonine KinasesRecQ HelicasesRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThreonineTranscription, GeneticCarrier ProteinsCell Cycle ProteinsGIP1 protein, S cerevisiaeIME2 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsNuclear ProteinsProtein KinasesProtein Phosphatase 1Protein Serine-Threonine KinasesRecQ HelicasesRepressor ProteinsSaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiaeSUM1 protein, S cerevisiaeThreonine

Identifiers

PMID17198398
PMCPMC2535912
OpenAlexW2069342373

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.