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Molecular and Cellular Biology, March 2004, p. 2277-2285, Vol. 24, No. 6
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.6.2277-2285.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Clb6/Cdc28 and Cdc14 Regulate Phosphorylation Status and Cellular Localization of Swi6

Marco Geymonat,^1, Ad Spanos,^1, Glenn P. Wells,^1,, Stephen J. Smerdon,² and Steven G. Sedgwick^1*

Divisions of Yeast Genetics,¹ Protein Structure, National Institute for Medical Research, London NW7 1AA, United Kingdom²

Received 9 October 2003/ Returned for modification 17 November 2003/ Accepted 29 December 2003

Nuclear export of the transcription factor Swi6 during the budding yeast Saccharomyces cerevisiae cell cycle is known to require phosphorylation of the Swi6 serine 160 residue. We show that Clb6/Cdc28 kinase is required for this nuclear export. Furthermore, Cdc28 combined with the S-phase cyclin Clb6 specifically phosphorylates serine 160 of Swi6 in vitro. Nuclear import of Swi6 occurs concomitantly with dephosphorylation of serine 160 in late M phase. We show that Cdc14 phosphatase, the principal effector of the mitotic exit network, can trigger nuclear import of Swi6 in vivo and that Cdc14 dephosphorylates Swi6 at serine 160 in vitro. Taken together, these observations show how Swi6 dephosphorylation and phosphorylation are integrated into changes of Cdc28 activity governing entry and exit from the G₁ phase of the cell cycle.

M.G., A.S., and G.P.W. contributed equally to this work.

Present address: The Wellcome Trust, London NW1 2BE, United Kingdom

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