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The Drosophila mitotic inhibitor Fruhstart specifically binds to the hydrophobic patch of cyclins.


ABSTRACT: The hydrophobic patch of cyclins interacts with cyclin-dependent kinase (Cdk) substrates and p27-type Cdk inhibitors. Although this interaction is assumed to contribute to the specificity of different Cdk-Cyclin complexes, its role in specific steps of the cell cycle has not been demonstrated. Here, we show that in Drosophila the mitotic inhibitor Frühstart (Frs) binds specifically and with high affinity to the hydrophobic patch of cyclins. In contrast to p27-type Cdk inhibitors, Frs does not form a stable interaction with the catalytic centre of Cdk and allows phosphorylation of generic model substrates, such as histone H1. Consistent with a 2.5 times stronger binding to CycA than to CycE in vitro, ectopic expression of frs induces endocycles, in a manner similar to that reported previously for downregulation of CycA or Cdk1. We propose that binding of Frs to cyclins blocks the hydrophobic patch to interfere with Cdk1 substrate recognition.

SUBMITTER: Gawlinski P 

PROVIDER: S-EPMC1866202 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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The Drosophila mitotic inhibitor Frühstart specifically binds to the hydrophobic patch of cyclins.

Gawliński Pawel P   Nikolay Rainer R   Goursot Catherine C   Lawo Steffen S   Chaurasia Bhagirath B   Herz Hans-Martin HM   Kussler-Schneider Yvonne Y   Ruppert Thomas T   Mayer Matthias M   Grosshans Jörg J  

EMBO reports 20070413 5


The hydrophobic patch of cyclins interacts with cyclin-dependent kinase (Cdk) substrates and p27-type Cdk inhibitors. Although this interaction is assumed to contribute to the specificity of different Cdk-Cyclin complexes, its role in specific steps of the cell cycle has not been demonstrated. Here, we show that in Drosophila the mitotic inhibitor Frühstart (Frs) binds specifically and with high affinity to the hydrophobic patch of cyclins. In contrast to p27-type Cdk inhibitors, Frs does not fo  ...[more]

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