Abstract
Protein-protein interactions (PPIs) play a central role in almost all cellular processes. Recent technological advances have enabled the elucidation of an incredibly complex PPI network within the cell. However, protein interactions driven by posttranslational modifications (PTMs) such as phosphorylation, which comprises a significant part of the PPI network, have proven difficult to decipher systematically. Herein, we describe a reciprocal protein-peptide array strategy to uncover PPIs mediated by tyrosine phosphorylation and the Src homology 2 (SH2) domain. This strategy, namely combining peptide and protein domain arrays for PPI mapping, may be applicable for other peptide-binding modules.
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Acknowledgments
This work was supported by grants (to S.S.C.L.) from the Canadian Cancer Society and the Ontario Research Fund. S.S.C.L. holds the Canada Research Chair in Functional Genomics and Cellular Proteomics.
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Liu, H., Voss, C., Li, S.S.C. (2017). Using Reciprocal Protein-Peptide Array Screening to Unravel Protein Interaction Networks. In: Machida, K., Liu, B. (eds) SH2 Domains. Methods in Molecular Biology, vol 1555. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6762-9_25
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DOI: https://doi.org/10.1007/978-1-4939-6762-9_25
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