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Molecular and Cellular Biology, June 2002, p. 3981-3993, Vol. 22, No. 12
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.12.3981-3993.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Protein Kinase A Operates a Molecular Switch That Governs Yeast Pseudohyphal Differentiation

Xuewen Pan and Joseph Heitman*

Departments of Genetics, Pharmacology and Cancer Biology, Microbiology, and Medicine, Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710

Received 19 November 2001/ Returned for modification 17 January 2002/ Accepted 18 March 2002

The yeast Saccharomyces cerevisiae undergoes a dimorphic filamentous transition in response to nutrient cues that is affected by both mitogen-activated protein kinase and cyclic AMP-protein kinase A signaling cascades. Here two transcriptional regulators, Flo8 and Sfl1, are shown to be the direct molecular targets of protein kinase A. Flo8 and Sfl1 antagonistically control expression of the cell adhesin Flo11 via a common promoter element. Phosphorylation by the protein kinase A catalytic subunit Tpk2 promotes Flo8 binding and activation of the Flo11 promoter and relieves repression by prohibiting dimerization and DNA binding by Sfl1. Our studies illustrate in molecular detail how protein kinase A combinatorially effects a key developmental switch. Similar mechanisms may operate in pathogenic fungi and more complex multicellular eukaryotic organisms.

* Corresponding author. Mailing address: 322 Carl Building, Box 3546, Research Dr., Duke University Medical Center, Durham, NC 27710. Phone: (919) 684-2824. Fax: (919) 684-5458. E-mail: heitm001{at}duke.edu.

Molecular and Cellular Biology, June 2002, p. 3981-3993, Vol. 22, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.12.3981-3993.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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