Abstract
It is apparent that most fundamental cellular processes are transduced through tyrosine kinase-mediated pathways involving the modification of tyrosine to phosphotyrosine. Therefore, for transduction without corruption, the protein-protein interactions involved have to be mutually exclusive. Many of these proteins bind via homologous domains whose binding characteristics suggest that their innate specificity is not sufficiently high to account for the integrity of signal transduction. Here two such phosphotyrosine-binding domains (Src homology 2 (SH2) and phosphotyrosine binding (PTB)) are described and their capability to impose the required level of specificity in a signal transduction pathway is analyzed. The data available suggest that the domains are not highly specific, and indeed in the case of the SH2 domain a high level of promiscuity is observed. How then is mutual exclusivity in signaling achieved? It appears that models other than linear pathways need to be invoked to gain an understanding of phosphotyrosine-mediated signal transduction.
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Ladbury, J.E. (2005). Protein-Protein Recognition in Phosphotyrosine-Mediated Intracellular Signaling. In: Waksman, G. (eds) Proteomics and Protein-Protein Interactions. Protein Reviews, vol 3. Springer, Boston, MA. https://doi.org/10.1007/0-387-24532-4_8
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DOI: https://doi.org/10.1007/0-387-24532-4_8
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