The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
The Ste5 Scaffold Allosterically Modulates Signaling Output of the Yeast Mating Pathway
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.
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Cites
A conserved docking motif in MAP kinases common to substrates, activators and regulators
Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E. (2000) · Nature Cell Biology · doi:10.1038/35000065 · Cited by 816
Rotation of photoreceptor clusters in the developing drosophila eye requires the nemo gene
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Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry
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A conserved protein interaction network involving the yeast MAP kinases Fus3 and Kss1
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Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451
Fuzzy Complexes: A More Stochastic View of Protein Function
Fuxreiter, M., & Tompa, P. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4614-0659-4_1 · Cited by 240
Docking interactions in protein kinase and phosphatase networks
Reményi, A., Good, M. C., & Lim, W. A. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.008 · Cited by 188
Self-citationDocking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2
Zhou, T., Sun, L., Humphreys, J., & Goldsmith, E. J. (2006) · Structure · doi:10.1016/j.str.2006.04.006 · Cited by 164
Substrate and Docking Interactions in Serine/Threonine Protein Kinases
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Metadata
- Authors
- Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., & Lim, W. A.
- Venue
- Science
- Published
- 2006-02-10
- Volume
- 311
- Issue
- 5762
- Pages
- 822-826
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2163680039
- Cited by
- 276
- References
- 6
- FWCI
- 10.44
- Type
- journal article
- Language
- en
- Open access
- closed
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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. https://doi.org/10.1126/science.1120941
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