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Molecular & Cellular Proteomics 2:1217-1224, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Functional Interaction Trap

A Strategy for Validating the Functional Consequences of Tyrosine Phosphorylation of Specific Substrates in Vivo^*

Alok Sharma, Susumu Antoku, Kosaku Fujiwara and Bruce J. Mayer

From the Department of Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, Connecticut 06030-3301

Protein tyrosine phosphorylation controls diverse signaling pathways, and disregulated tyrosine kinase activity plays a direct role in human diseases such as cancer. Because activated kinases exert their effects by phosphorylating multiple substrate proteins, it is difficult or impossible to assess experimentally the contribution of a particular substrate to a cellular response or activity. To overcome this problem, we have developed a novel approach termed the "functional interaction trap," in which two proteins are induced to interact in a pairwise fashion through an engineered, highly specific binding interface. We show that the functional interaction trap can be used to direct a modified tyrosine kinase to specifically phosphorylate a single substrate of choice in vivo, permitting analysis of the resulting biological output. This strategy provides a powerful tool for validating the functional significance of tyrosine phosphorylation and other post-translational modifications identified by proteomic discovery efforts.

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