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Submitted on August 18, 2003
Revised on September 23, 2003
Accepted on September 29, 2003

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

Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, CT 06030-3301

Corresponding Author: bmayer{at}neuron.uchc.edu

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" (FIT), in which two proteins are induced to interact in a pairwise fashion through an engineered, highly specific binding interface. We show that FIT 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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