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

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.

authors

Barberis M,Pagano MA,Gioia LD,Marin O,Vanoni M,Pinna LA,Alberghina L

doi

10.1016/j.bbrc.2005.08.224

subject

Has Abstract

pub_date

2005-11-04 00:00:00

pages

1040-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01921-2

journal_volume

336

pub_type

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