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Rewiring MAP Kinase Pathways Using Alternative Scaffold Assembly Mechanisms

Science  14 Feb 2003:
Vol. 299, Issue 5609, pp. 1061-1064
DOI: 10.1126/science.1076979

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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.

  • * To whom correspondence should be addressed. E-mail: wlim{at}itsa.ucsf.edu

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