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Molecular and Cellular Biology, January 2002, p. 57-68, Vol. 22, No. 1
0270-7306/01/$04.00+0     DOI: 10.1128/MCB.22.1.57-68.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

CAK1 Promotes Meiosis and Spore Formation in Saccharomyces cerevisiae in a CDC28-Independent Fashion

Michael Schaber,1,{dagger} Anne Lindgren,1 Karen Schindler,1 David Bungard,1 Philipp Kaldis,2 and Edward Winter1*

Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107,1 Regulation of Cell Growth Laboratory, National Cancer Institute, Frederick, Maryland 217022

Received 13 July 2001/ Returned for modification 28 August 2001/ Accepted 7 October 2001

CAK1 encodes a protein kinase in Saccharomyces cerevisiae whose sole essential mitotic role is to activate the Cdc28p cyclin-dependent kinase by phosphorylation of threonine-169 in its activation loop. SMK1 encodes a sporulation-specific mitogen-activated protein (MAP) kinase homolog that is required to regulate the postmeiotic events of spore wall assembly. CAK1 was previously identified as a multicopy suppressor of a weakened smk1 mutant and shown to be required for spore wall assembly. Here we show that Smk1p, like other MAP kinases, is phosphorylated in its activation loop and that Smk1p is not activated in a cak1 missense mutant. Strains harboring a hyperactivated allele of CDC28 that is CAK1 independent and that lacks threonine-169 still require CAK1 to activate Smk1p. The data indicate that Cak1p functions upstream of Smk1p by activating a protein kinase other than Cdc28p. We also found that mutants lacking CAK1 are blocked early in meiotic development, as they show substantial delays in premeiotic DNA synthesis and defects in the expression of sporulation-specific genes, including IME1. The early meiotic role of Cak1p, like the postmeiotic role in the Smk1p pathway, is CDC28 independent. The data indicate that Cak1p activates multiple steps in meiotic development through multiple protein kinase targets.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, PA 19107. Phone: (215) 503-4139. Fax: (215) 923-9162. E-mail: winter{at}lac.jci.tju.edu.

{dagger} Present address: Merck Research Laboratories, Cancer Research Department, West Point, PA 19486.

Molecular and Cellular Biology, January 2002, p. 57-68, Vol. 22, No. 1
0022-538X/01/$04.00+0     DOI: 10.1128/MCB.22.1.57-68.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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