Persistent nuclear accumulation of protein kinase CK2 during the G1-phase of the cell cycle does not depend on the ERK1/2 pathway but requires active protein synthesis

Francesc A. Miro, Franc Llorens, Nerea Roher, Maria Plana, Néstor Gómez, Emilio Itarte

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

Protein kinase CK2 and phosphorylated ERK1/2 accumulated in nucleus after serum stimulation of quiescent HepG2 cells. Nonetheless, phospho-ERK1/2 accumulated mainly in the nuclease-extracted fraction (NE) whereas the increases in nuclear CK2 (either CK2α or CK2β) occurred initially in the nuclease-resistant fraction (NR). Transient decreases in CK2 were observed in cytoplasm and NE in the first 3 h but thereafter they either reverted (cytoplasm) or increased above the control (NE). CK2 levels in both NE and NR were high in cells arrested at G1/S. Maximal nuclearaccumulation of CK2 was blocked by cycloheximide but little affected by PD98059, SB203580 or apigenin, all of which affected nuclear phopho-ERK1/2. Thus, nuclear accumulation of CK2 during G1 phase is independent of ERK1/2 pathway. Although this process may initially relay on intracellular redistribution of the preexisting enzyme, active protein synthesis is required to attain maximal nuclear CK2 levels. © 2002 Elsevier Science (USA). All rights reserved.
Original languageEnglish
Pages (from-to)165-172
JournalArchives of Biochemistry and Biophysics
Volume406
DOIs
Publication statusPublished - 6 Nov 2002

Keywords

  • CK2
  • Cell cycle
  • ERK1/2
  • HepG2 cells
  • Serum stimulation
  • p53

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