ArticleProceedings of the National Academy of Sciences of the United States of America2011
Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Not your Mother's MAPKs: Apicomplexan MAPK function in daughter cell budding.PLoS pathogens · 2022Review
- Correlation Between Improved Mating Efficiency and Weakened Scaffold-Kinase Interaction in the Mating Pheromone Response Pathway Revealed by Interspecies Complementation.Frontiers in microbiology · 2022Article
- Determination of the molecular reach of the protein tyrosine phosphatase SHP-1.Biophysical journal · 2021Article
- The Influence of Molecular Reach and Diffusivity on the Efficacy of Membrane-Confined Reactions.Biophysical journal · 2019Article
- Single-molecule localization microscopy and tracking with red-shifted states of conventional BODIPY conjugates in living cells.Nature communications · 2019Article
- Comprehensive profiling of the STE20 kinase family defines features essential for selective substrate targeting and signaling output.PLoS biology · 2019Article
- Dissection of MAPK signaling specificity through protein engineering in a developmental context.BMC plant biology · 2018Article
- Biophysical assay for tethered signaling reactions reveals tether-controlled activity for the phosphatase SHP-1.Science advances · 2017Article
- Engineering dynamical control of cell fate switching using synthetic phospho-regulons.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Rewiring MAP kinases in Saccharomyces cerevisiae to regulate novel targets through ubiquitination.eLife · 2016Article
- The calcineurin signaling network evolves via conserved kinase-phosphatase modules that transcend substrate identity.Molecular cell · 2014Article
- Exploiting holistic approaches to model specificity in protein phosphorylation.Frontiers in genetics · 2014Review
- Regulation of NKCC2 activity by inhibitory SPAK isoforms: KS-SPAK is a more potent inhibitor than SPAK2.American journal of physiology. Renal physiology · 2013Article
- Receptor tyrosine kinases fall into distinct classes based on their inferred signaling networks.Science signaling · 2013Article
- Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) module.The Journal of biological chemistry · 2013Article
- Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Evaluation and properties of the budding yeast phosphoproteome.Molecular & cellular proteomics : MCP · 2012Article
- Designing orthogonal signaling pathways: how to fit in with the surroundings.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Phosphosite mapping of P-type plasma membrane H+-ATPase in homologous and heterologous environments.The Journal of biological chemistry · 2012Article
- The secret life of kinases: functions beyond catalysis.Cell communication and signaling : CCS · 2011Article
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3 authors.
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Abstract
The yeast Saccharomyces cerevisae has four distinct mitogen-activated protein kinase kinases (MAPKKs), each of which has a distinct functional identity characterized by communication with specific upstream and downstream partners to form distinct functional pathways. These four kinases belong to one family, sharing closely related catalytic domains. How have these four related kinases diverged to take on four distinct functional roles? The specificity of an enzyme for a particular substrate is often thought to reside in differences in the catalytic domain. However, many kinases, including MAPKKs, have modular interaction domains and motifs that have been shown to play an important role in determining the specificity of kinases through recruitment to specific partners and complexes. Here we probe the relative importance of catalytic domain interactions versus recruitment interactions in defining the functional identity of MAPKKs by asking whether we can use recruitment interactions to force other MAPKK catalytic domains to play the functional role of the mating MAPKK, Ste7. We find that two alternative MAPKKs, Pbs2 and Mkk2, can be forced to functionally replace the mating MAPKK Ste7, but only if the proper set of recruitment interactions are grafted onto their catalytic domains. These results show that within a family of kinases, recruitment interactions can play a dominant role in defining functional identity, and is consistent with a model in which new kinase functions can arise through recombination of existing catalytic domains with new interaction modules.
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