We have previously demonstrated that the cyclin-dependent kinase inhibitor (Cki) Sic1 of Saccharomyces cerevisiae is phosphorylated in vitro by the CK2 kinase on Ser(201) residue. Moreover, we have collected evidence showing that Sic1 is functionally and structurally related to mammalian Cki p27(Kip1) and binds to the mammalian Cdk2/cyclin A complex with a similar mode of inhibition. In this paper, we use SPR analysis to investigate the binding of Sic1 to the catatytic and regulatory subunits of CK2. Evidence is presented showing that phosphorylation of Sic1 at the CK2 consensus site QES(201)EDEED increases the binding of a Sic1-derived peptide to the Cdk2/cyclin A complex, a functional homologue of the yeast Cdk1/Clb5,6. Moreover, Sic1 fully phosphorylated in vitro on Ser(201) by CK2 is shown to be a stronger inhibitor of the Cdk/cyclin complexes than the unphosphorylated protein. Taken together, these data disclose the possibility that CK2 plays a role in the regulation of Sic1 activity.

Barberis, M., Pagano, M., Gioia, L., Marin, O., Vanoni, M., Pinna, L., et al. (2005). CK2 regulates in vitro the activity of the yeast cyclin-dependent kinase inhibitor Sic1. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 336(4), 1040-1048 [10.1016/j.bbrc.2005.08.224].

CK2 regulates in vitro the activity of the yeast cyclin-dependent kinase inhibitor Sic1

Gioia, LD;VANONI, MARCO ERCOLE;ALBERGHINA, LILIA
2005

Abstract

We have previously demonstrated that the cyclin-dependent kinase inhibitor (Cki) Sic1 of Saccharomyces cerevisiae is phosphorylated in vitro by the CK2 kinase on Ser(201) residue. Moreover, we have collected evidence showing that Sic1 is functionally and structurally related to mammalian Cki p27(Kip1) and binds to the mammalian Cdk2/cyclin A complex with a similar mode of inhibition. In this paper, we use SPR analysis to investigate the binding of Sic1 to the catatytic and regulatory subunits of CK2. Evidence is presented showing that phosphorylation of Sic1 at the CK2 consensus site QES(201)EDEED increases the binding of a Sic1-derived peptide to the Cdk2/cyclin A complex, a functional homologue of the yeast Cdk1/Clb5,6. Moreover, Sic1 fully phosphorylated in vitro on Ser(201) by CK2 is shown to be a stronger inhibitor of the Cdk/cyclin complexes than the unphosphorylated protein. Taken together, these data disclose the possibility that CK2 plays a role in the regulation of Sic1 activity.
Articolo in rivista - Articolo scientifico
Surface Plasmon Resonance; Saccharomyces cerevisiae; Cyclin-Dependent Kinase 2; Saccharomyces cerevisiae Proteins; Protein Subunits; Models, Molecular; Cyclin A; Kinetics; Amino Acids; Enzyme Activation; Thermodynamics; Cyclin-Dependent Kinase Inhibitor Proteins; Phosphorylation; Casein Kinase II; Protein Binding
English
4-nov-2005
336
4
1040
1048
none
Barberis, M., Pagano, M., Gioia, L., Marin, O., Vanoni, M., Pinna, L., et al. (2005). CK2 regulates in vitro the activity of the yeast cyclin-dependent kinase inhibitor Sic1. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 336(4), 1040-1048 [10.1016/j.bbrc.2005.08.224].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/15401
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