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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2000

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Phosphorylation of Cdc28 and regulation of cell size by the protein kinase CKII in Saccharomyces cerevisiae

Anno di pubblicazione: 2000

Formato: Cartaceo

Autori: Russo, G.L. and Van den Bos, C. and Sutton, A. and Coccetti, P. and Baroni, M.D. and Alberghina, L. and Marshak, D.R.

Affiliazioni autori: Ist. di Scienze dell'Alimentazione, via Roma 52 A/C, Avellino 83100, Italy

Autori CNR:


Lingua: inglese

Abstract: The CDK (cyclin-dependent kinase) family of enzymes is required for the G 1-to-S-phase and G 2-to-M-phase transitions during the cell-division cycle of eukaryotes. We have shown previously that the protein kinase CKII catalyses the phosphorylation of Ser-39 in Cdc2 during the G 1 phase of the HeLa cell-division cycle [Russo, Vandenberg, Yu, Bae, Franza and Marshak (1992) J. Biol. Chem. 267, 20317-20325]. To identify a functional role for this phosphorylation, we have studied the homologous enzymes in the budding yeast Saccharomyces cerevisiae. The S. cerevisiae homologue of Cdc2, Cdc28, contains a consensus CKII site (Ser-46), which is homologous with that of human Cdc2. Using in vitro kinase assays, metabolic labelling, peptide mapping and phosphoamino acid analysis, we demonstrate that this site is phosphorylated in Cdc28 in vivo as well in vitro. In addition, S. cerevisiae cells in which Ser-46 has been mutated to alanine show a decrease in both cell volume and protein content of 33%, and this effect is most pronounced in the stationary phase. Because cell size in S. cerevisiae is regulated primarily at the G 1 stage, we suggest that CKII contributes to the regulation of the cell cycle in budding yeast by phosphorylation of Cdc28 as a checkpoint for G 1 progression.

Lingua abstract: inglese

Pagine da: 143

Pagine a: 150

Pagine totali: 8


Biochemical journal Biochemical Society,
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 0264-6021

Numero volume: 351

Numero fascicolo: 1

DOI: 10.1042/0264-6021:3510143

Referee: Sė: Internazionale

Indicizzato da:

  • Scopus [2-s2.0-0034306416]
  • PubMed [10998356]

Parole chiave:

  • casein kinase II
  • cyclin dependent kinase
  • amino acid analysis
  • amino acid substitution
  • article
  • cell cycle
  • cell cycle G1 phase
  • cell cycle G2 phase
  • cell cycle S phase
  • cell size
  • cell volume
  • controlled study
  • enzyme phosphorylation
  • HeLa cell
  • in vitro study
  • in vivo study
  • metaphase
  • nonhuman
  • peptide mapping
  • priority journal
  • protein content
  • Saccharomyces cerevisiae
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Blotting
  • Western
  • CDC28 Protein Kinase
  • Cell Division
  • Flow Cytometry
  • Molecular Sequence Data
  • Mutation
  • Peptide Mapping
  • Phosphorylation
  • Phosphoserine
  • Protein-Serine-Threonine Kinases
  • Saccharomyces cerevisiae
  • Sequence Alignment
  • Support
  • Non-U.S. Gov't
  • Support
  • U.S. Gov't
  • P.H.S.
  • Saccharomyces cerevisiae

URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-0034306416&partnerID=40&md5=ea1563a8f9b5a28538f1af2de0e20691

Altre informazioni: cited By (since 1996)18 PDF scaricabile gratuitamente al sito: http://www.biochemj.org/bj/351/bj3510143.htm

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