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Biochem Biophys Res Commun. 2006 Aug 4;346(3):786-93. Epub 2006 Jun 6.

Sic1 is phosphorylated by CK2 on Ser201 in budding yeast cells.

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  • 1Dipartimento di Biotecnologie e Bioscienze, Universit√† degli Studi Milano-Bicocca, P.zza della Scienza 2, 20126 Milano, Italy. paola.coccetti@unimib.it

Abstract

We have previously identified Ser201 of Sic1, a yeast cyclin-dependent kinase inhibitor, as an in vitro target of protein kinase CK2. Here we present new evidence, by using specific anti-P-Ser201 antibodies and 2-D gel electrophoresis coupled to MALDI mass spectrometry analysis, that Sic1 is phosphorylated in vivo on Ser201 shortly after its de novo synthesis, during late anaphase in glucose-grown cells. This phosphorylation is also detected in Sic1 immunopurified from G1 cells. In agreement with these data we also show that the catalytic alpha' subunit of CK2, whose function is required for cell cycle progression, is detected in Sic1 immunopurified complexes, and that phosphorylation on Ser201 is reduced after CK2 inactivation at the non-permissive temperature in a cka1delta cka2(ts) yeast strain. These data strongly support the notion that CK2 phosphorylates Sic1 in vivo.

PMID:
16777072
DOI:
10.1016/j.bbrc.2006.05.171
[PubMed - indexed for MEDLINE]
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