Editors' ChoiceProtein Interaction

Flexible Management

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Science's STKE  18 Feb 2003:
Vol. 2003, Issue 170, pp. tw75-TW75
DOI: 10.1126/stke.2003.170.tw75

Scaffolding proteins contain binding sites for individual components of signal pathways and are thought to serve as grand organizing centers. Park et al. (see the Perspective by Ptashne and Gann) explored the basic physical requirements for a scaffold recruitment interaction using the yeast mitogen-activating protein kinase (MAPK) signaling pathways as a model system. Replacing defective scaffold-kinase recruitment interactions with completely different protein-protein interactions restored proper signaling, thus demonstrating the tremendous plasticity of these organizing factors. Such flexibility likely underlies the evolution of new pathways and resembles that of binding sites in transcription factors.

S.-H. Park, A. Zarrinpar, W. A. Lim, Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms. Science 299, 1061-1064 (2003). [Abstract] [Full Text]

M. Ptashne, A. Gann, Imposing specificity on kinases. Science 299, 1025-1027 (2003). [Summary] [Full Text]

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