Nutrient sensing kinases PKA and sch9 phosphorylate the catalytic domain of the ubiquitin-conjugating enzyme Cdc34

Ross Cocklin, Mark Goebl

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Cell division is controlled in part by the timely activation of the CDK, Cdc28, through its association with G1 and G2 cyclins. Cdc28 complexes are regulated in turn by the ubiquitin conjugating enzyme Cdc34 and SCF ubiquitin ligase complexes of the ubiquitin-proteasome system (UPS) to control the initiation of DNA replication. Here we demonstrate that the nutrient sensing kinases PKA and Sch9 phosphorylate S97 of Cdc34. S97 is conserved across species and restricted to the catalytic domain of Cdc34/Ubc7-like E2s. Cdc34-S97 phosphorylation is cell cycle regulated, elevated during active cell growth and division and decreased during cell cycle arrest. Cell growth and cell division are orchestrated to maintain cell size homeostasis over a wide range of nutrient conditions. Cells monitor changes in their environment through nutrient sensing protein kinases. Thus Cdc34 phosphorylation by PKA and Sch9 provides a direct tether between G1 cell division events and cell growth.

Original languageEnglish
Article numbere27099
JournalPLoS One
Volume6
Issue number11
DOIs
StatePublished - Nov 7 2011

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Ubiquitin-Conjugating Enzymes
ubiquitin-protein ligase
active sites
Cell Division
Nutrients
cell division
Catalytic Domain
phosphotransferases (kinases)
Phosphotransferases
Cells
Cell growth
Food
cell growth
nutrients
ubiquitin
Phosphorylation
Cyclin G2
phosphorylation
SKP Cullin F-Box Protein Ligases
Growth

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Nutrient sensing kinases PKA and sch9 phosphorylate the catalytic domain of the ubiquitin-conjugating enzyme Cdc34. / Cocklin, Ross; Goebl, Mark.

In: PLoS One, Vol. 6, No. 11, e27099, 07.11.2011.

Research output: Contribution to journalArticle

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