Carboxyl-terminal domain of p27(Kip1) activates CDC2

Aykut Üren, J. Jakus, Jaime Font De Mora, Andrew Yeudall, Eugenio Santos, Silvio Gutkind, Mohammad A. Heidaran

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

A variant form of p27 was unexpectedly detected in a synchronized culture of NIH3T3 cells treated with serum. The expression levels of this form of p27 which lacked its amino (NH2)-terminal region reached maximum during G2/M phase. Since the appearance of the NH2-terminal truncated form of p27 coincided with increased expression of Cdc2, we hypothesized that p27 may play a role in regulating Cdc2 catalytic activity. To test this hypothesis, wild type p27, as well as the amino-terminal (Np27) and carboxyl- terminal (Cp27), were individually expressed, purified, and examined for their ability to regulate CDC2 kinase activity in vitro. Our data showed that both p27 and Np27 inhibited CDC2 kinase activity. However, in marked contrast, Cp27 enhanced the CDC2 kinase activity. In vitro kinase assays showed that Cp27 and p27 were phosphorylated by CDC2, whereas Np27 was not. In addition, we demonstrated that deletion of the putative CDC2 phosphorylation site in the carboxyl-terminal domain of Cp27 diminished activation of CDC2 kinase activity otherwise stimulated by Cp27. A similar deletion did not have any effect on the inhibitory function of p27. Together these results suggest that the carboxyl-terminal domain of p27 may activate CDC2 kinase activity in vivo during G2/M and that this effect may be regulated by serine/threonine phosphorylation.

Original languageEnglish
Pages (from-to)21669-21672
Number of pages4
JournalJournal of Biological Chemistry
Volume272
Issue number35
DOIs
Publication statusPublished - Aug 29 1997

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Phosphotransferases
Phosphorylation
G2 Phase
Threonine
Cell Division
Serine
Assays
Catalyst activity
Cell Culture Techniques
Chemical activation
Serum
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry

Cite this

Üren, A., Jakus, J., De Mora, J. F., Yeudall, A., Santos, E., Gutkind, S., & Heidaran, M. A. (1997). Carboxyl-terminal domain of p27(Kip1) activates CDC2. Journal of Biological Chemistry, 272(35), 21669-21672. https://doi.org/10.1074/jbc.272.35.21669

Carboxyl-terminal domain of p27(Kip1) activates CDC2. / Üren, Aykut; Jakus, J.; De Mora, Jaime Font; Yeudall, Andrew; Santos, Eugenio; Gutkind, Silvio; Heidaran, Mohammad A.

In: Journal of Biological Chemistry, Vol. 272, No. 35, 29.08.1997, p. 21669-21672.

Research output: Contribution to journalArticle

Üren, A, Jakus, J, De Mora, JF, Yeudall, A, Santos, E, Gutkind, S & Heidaran, MA 1997, 'Carboxyl-terminal domain of p27(Kip1) activates CDC2', Journal of Biological Chemistry, vol. 272, no. 35, pp. 21669-21672. https://doi.org/10.1074/jbc.272.35.21669
Üren A, Jakus J, De Mora JF, Yeudall A, Santos E, Gutkind S et al. Carboxyl-terminal domain of p27(Kip1) activates CDC2. Journal of Biological Chemistry. 1997 Aug 29;272(35):21669-21672. https://doi.org/10.1074/jbc.272.35.21669
Üren, Aykut ; Jakus, J. ; De Mora, Jaime Font ; Yeudall, Andrew ; Santos, Eugenio ; Gutkind, Silvio ; Heidaran, Mohammad A. / Carboxyl-terminal domain of p27(Kip1) activates CDC2. In: Journal of Biological Chemistry. 1997 ; Vol. 272, No. 35. pp. 21669-21672.
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