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Park SH, et al.  (2003) Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms. Science 299(5609):1061-4

Abstract: How scaffold proteins control information flow in signaling pathways is poorly understood: Do they simply tether components, or do they precisely orient and activate them? We found that the yeast mitogen-activated protein (MAP) kinase scaffold Ste5 is tolerant to major stereochemical perturbations; heterologous protein interactions could functionally replace native kinase recruitment interactions, indicating that simple tethering is largely sufficient for scaffold-mediated signaling. Moreover, by engineering a scaffold that tethers a unique kinase set, we could create a synthetic MAP kinase pathway with non-natural input-output properties. These findings demonstrate that scaffolds are highly flexible organizing factors that can facilitate pathway evolution and engineering.

Status: Published Type: Journal Article PubMed ID: 12511654

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FUS3 HOG1 PBS2 SHO1 STE11 STE5 STE7
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