Dissociation of p34cdc2 complex formation from phosphorylation and histone H1 kinase activity

Scott T. Eblen, Michael P. Fautsch, Michael P Fautsch, Melissa Snyder, Edward B Leof

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The cell cycle inhibitor mimosine was used to examine the activation of the p34cdc2 protein kinase in S phase of the cell cycle. Addition of mimosine to cycling epithelial cells halted cell cycle traverse in S phase, coincident with an inhibition of p34cdc2 histone H1 kinase activity. Mimosine treatment did not alter p34cdc2 synthesis or turnover; however, overall phosphorylation of p34cdc2 was decreased to near undetectable levels. Although activity of p34cdc2 was inhibited, the ability of the protein to form high molecular weight complexes, a phenomenon associated with kinase activation in vivo, was not affected. These results indicate that p34cdc2 complex formation can occur in the absence of phosphorylation and that phosphorylation of p34cdc2 is then required to activate these preformed complexes.

Original languageEnglish (US)
Pages (from-to)1994-2000
Number of pages7
JournalCancer Research
Volume55
Issue number9
StatePublished - May 1 1995

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Mimosine
Cell Cycle
Phosphorylation
S Phase
CDC2 Protein Kinase
Protein Kinases
Phosphotransferases
Molecular Weight
Epithelial Cells
histone H1 kinase
Proteins

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

Dissociation of p34cdc2 complex formation from phosphorylation and histone H1 kinase activity. / Eblen, Scott T.; Fautsch, Michael P.; Fautsch, Michael P; Snyder, Melissa; Leof, Edward B.

In: Cancer Research, Vol. 55, No. 9, 01.05.1995, p. 1994-2000.

Research output: Contribution to journalArticle

Eblen, Scott T. ; Fautsch, Michael P. ; Fautsch, Michael P ; Snyder, Melissa ; Leof, Edward B. / Dissociation of p34cdc2 complex formation from phosphorylation and histone H1 kinase activity. In: Cancer Research. 1995 ; Vol. 55, No. 9. pp. 1994-2000.
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