Evidence map›Paper›PMID 15282298›Full record

ArticleMolecular and cellular biology2004

The in vivo activity of Ime1, the key transcriptional activator of meiosis-specific genes in Saccharomyces cerevisiae, is inhibited by the cyclic AMP/protein kinase A signal pathway through the glycogen synthase kinase 3-beta homolog Rim11.

Ifat Rubin-Bejerano, Shira Sagee, Osnat Friedman, Lilach Pnueli, Yona Kassir

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Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

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26citing papers in PubMed
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1 · What the graph read from it

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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

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Ifat Rubin-BejeranoDepartment of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel. ykassir@techunix.technion.ac.il
Shira Sagee
Osnat Friedman
Lilach Pnueli
Yona Kassir

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation is the main mode by which signals are transmitted to key regulators of developmental pathways. The glycogen synthase kinase 3 family plays pivotal roles in the development and well-being of all eukaryotic organisms. Similarly, the budding yeast homolog Rim11 is essential for the exit of diploid cells from the cell cycle and for entry into the meiotic developmental pathway. In this report we show that in vivo, in cells grown in a medium promoting vegetative growth with acetate as the sole carbon source (SA medium), Rim11 phosphorylates Ime1, the master transcriptional activator required for entry into the meiotic cycle and for the transcription of early meiosis-specific genes. We demonstrate that in the presence of glucose, the kinase activity of Rim11 is inhibited. This inhibition could be due to phosphorylation on Ser-5, Ser-8, and/or Ser-12 because in the rim11S5AS8AS12A mutant, Ime1 is incorrectly phosphorylated in the presence of glucose and cells undergo sporulation. We further show that this nutrient signal is transmitted to Rim11 and consequently to Ime1 by the cyclic AMP/protein kinase A signal transduction pathway. Ime1 is phosphorylated in SA medium on at least two residues, Tyr-359 and Ser-302 and/or Ser-306. Ser-302 and Ser-306 are part of a consensus site for the mammalian homolog of Rim11, glycogen synthase kinase 3-beta. Phosphorylation on Tyr-359 but not Ser-302 or Ser-306 is essential for the transcription of early meiosis-specific genes and sporulation. We show that Tyr-359 is phosphorylated by Rim11.

Indexed as

AcetatesCulture MediaCyclic AMPCyclic AMP-Dependent Protein KinasesGene Expression Regulation, FungalGlucoseGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaIntracellular Signaling Peptides and ProteinsMeiosisNitrogenNuclear ProteinsPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesSaccharomyces cerevisiaeAcetatesCulture MediaCyclic AMPCyclic AMP-Dependent Protein KinasesGlucoseGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaIME1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsNitrogenNuclear ProteinsProtein Serine-Threonine KinasesRIM11 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerineTranscription FactorsTyrosine

Identifiers

PMID15282298
PMCPMC479714

What OpenQuestion holds

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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.