The cell wall integrity signalling MAP kinase of Saccharomyces cerevisiae, Slt2p/Mpk1p, is activated in response to cell wall stress. Slt2 and its mammalian orthologue ERK5 are unusual among MAP kinases, in that they possess the ability to activate transcription of a GAL1-lacZ reporter when fused to the DNA-binding domain of the Gal4 transcription factor. In this study, we demonstrate that transcriptional activation of a Gal4-Slt2p fusion is responsive to cell wall stress and requires phosphorylation of Slt2p. We identify two neighbouring but separable transcription activation domains within the C-terminal half of Slt2p. Additionally, we present data suggesting that intramolecular interactions controlled by phosphorylation of Slt2p regulate the function of these domains, which are masked by the N-terminal catalytic domain under inactive conditions. Finally, we demonstrate that Slt2p self-associates, probably through a glutamine-rich region within the C-terminal half of the protein.

• PMID: 17397108
• DOI full text
• PubMed
• PubTator

Reference Type

Journal Article | Research Support, N.I.H., Extramural | Research Support, Non-U.S. Gov't

Authors

Kim KY, Cosano IC, Levin DE, Molina M, Martín H

Primary Lit For

Additional Lit For

Review For