The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway

Roby P. Bhattacharyya, Attila Reményi, Matthew C. Good, Caleb J. Bashor, Arnold M. Falick, Wendell A. Lim

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203 Citations (Scopus)

Abstract

Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.

Original languageEnglish
Pages (from-to)822-826
Number of pages5
JournalScience
Volume311
Issue number5762
DOIs
Publication statusPublished - Feb 10 2006

ASJC Scopus subject areas

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    Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., & Lim, W. A. (2006). The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway. Science, 311(5762), 822-826. https://doi.org/10.1126/science.1120941