Hyperphosphorylation of the N-terminal domain of cdc25 regulates activity toward cyclin B1/cdc2 but not cyclin A/cdk2

Gabrielli B.G., Clark J.M., McCormack A.K. and Ellem K.A.O. (1997) Hyperphosphorylation of the N-terminal domain of cdc25 regulates activity toward cyclin B1/cdc2 but not cyclin A/cdk2. Journal of Biological Chemistry, 272 45: 28607-28614. doi:10.1074/jbc.272.45.28607

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Author Gabrielli B.G.
Clark J.M.
McCormack A.K.
Ellem K.A.O.
Title Hyperphosphorylation of the N-terminal domain of cdc25 regulates activity toward cyclin B1/cdc2 but not cyclin A/cdk2
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 1997-11-07
Year available 1997
Sub-type Article (original research)
DOI 10.1074/jbc.272.45.28607
Open Access Status File (Publisher version)
Volume 272
Issue 45
Start page 28607
End page 28614
Total pages 8
Place of publication BETHESDA
Publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Language eng
Subject 1303 Specialist Studies in Education
Abstract Cdc25 regulates entry into mitosis by regulating the activation of cyclin B/cdc2. In humans, at least two cdc25 isoforms have roles in controlling the G(2)/M transition. Here we show, using bacterially expressed recombinant proteins, that two cdc25B splice variants, cdc25B2 and cdc25B3, are capable of activating cyclin A/cdk2 and cyclin B/cdc2, but that mitotic hyperphosphorylation of these proteins increases their activity toward only cyclin B1/cdc2, Cdc25C has only very low activity in its unphosphorylated form, add following hyperphosphorylation it will efficiently catalyze the activation of only cyclin B/cdc2, This was reflected by the in vivo activity of the immunoprecipitated cdc25B and cdc25C from interphase and mitotic HeLa cells. The increased activity of the hyperphosphorylated cdc25s toward cyclin B1/cdc2 was in large part due to increased binding of this substrate. The substrate specificity, activities; and timing of the hyperphosphorylation of cdc25B and cdc25C during G(2) and M suggest that these two mitotic cdc25 isoforms are activated by different kinases and perform different functions during progression through G(2) into mitosis.
Keyword Biochemistry & Molecular Biology
Biochemistry & Molecular Biology
BIOCHEMISTRY & MOLECULAR BIOLOGY
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
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