Cell cycle regulation of the p34cdc2 inhibitory kinases

Atherton-Fessler, Sue, Liu, Feng, Gabrielli, Brian, Lee, Margaret S., Peng, Cheng-Yuan and Piwnica-Worms, Helen (1994) Cell cycle regulation of the p34cdc2 inhibitory kinases. Molecular Biology of the Cell, 5 9: 989-1001. doi:10.1091/mbc.5.9.989

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Author Atherton-Fessler, Sue
Liu, Feng
Gabrielli, Brian
Lee, Margaret S.
Peng, Cheng-Yuan
Piwnica-Worms, Helen
Title Cell cycle regulation of the p34cdc2 inhibitory kinases
Formatted title
Cell cycle regulation of the p34cdc2 inhibitory kinases
Journal name Molecular Biology of the Cell   Check publisher's open access policy
ISSN 1059-1524
Publication date 1994-09
Sub-type Article (original research)
DOI 10.1091/mbc.5.9.989
Open Access Status File (Publisher version)
Volume 5
Issue 9
Start page 989
End page 1001
Total pages 13
Place of publication Bethesda, MD, United States
Publisher American Society for Cell Biology
Language eng
Formatted abstract
In cells of higher eukaryotic organisms the activity of the p34cdc2/cyclin B complex is inhibited by phosphorylation of p34cdc2 at two sites within its amino-terminus (threonine 14 and tyrosine 15). In this study, the cell cycle regulation of the kinases responsible for phosphorylating p34cdc2 on Thr14 and Tyr15 was examined in extracts prepared from both HeLa cells and Xenopus eggs. Both Thr14- and Tyr15- specific kinase activities were regulated in a cell cycle-dependent manner. The kinase activities were high throughout interphase and diminished coincident with entry of cells into mitosis. In HeLa cells delayed in G2 by the DNA-binding dye Hoechst 33342, Thr14- and Tyr15- specific kinase activities remained high, suggesting that a decrease in Thr14- and Tyr15- kinase activities may be required for entry of cells into mitosis. Similar cell cycle regulation was observed for the Thr14/Tyr15 kinase(s) in Xenopus egg extracts. These results indicate that activation of CDC2 and entry of cells into mitosis is not triggered solely by activation of the Cdc25 phosphatase but by the balance between Thr14/Tyr15 kinase and phosphatase activities. Finally, we have detected two activities capable of phosphorylating p34cdc2 on Thr14 and/or Tyr15 in interphase extracts prepared from Xenopus eggs. An activity capable of phosphorylating Tyr15remained soluble after ultracentrifugation of interphase extracts whereas a second activity capable of phosphorylating both Thr14 and Tyr15pelleted. The pelleted fraction contained activities that were detergent extractable and that phosphorylated p34cdc2 on both Thr14 and Tyr15. The Thr14- and Tyr15-specific kinase activities co-purified through three successive chromatographic steps indicating the presence of a dual-specificity protein kinase capable of acting on p34cdc2.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Mater Research Institute-UQ (MRI-UQ)
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