Recognition and specificity in protein tyrosine kinase-mediated signalling
Z Songyang, LC Cantley - Trends in biochemical sciences, 1995 - cell.com
Z Songyang, LC Cantley
Trends in biochemical sciences, 1995•cell.comThere are several factors that contribute to the specificities of protein tyrosine kinases (PTKs)
in signal transduction pathways. While protein-protein interaction domains, such as the Src
homology (SH2 and SH3) domains, regulate the cellular localization of PTKs and their
substrates, the specificities of PTKs are ultimately determined by their catalytic domains. The
use of peptide libraries has revealed the substrate specificities of SH2 domains and PTK
catalytic domains, and has suggested cross-talk between these domains.
in signal transduction pathways. While protein-protein interaction domains, such as the Src
homology (SH2 and SH3) domains, regulate the cellular localization of PTKs and their
substrates, the specificities of PTKs are ultimately determined by their catalytic domains. The
use of peptide libraries has revealed the substrate specificities of SH2 domains and PTK
catalytic domains, and has suggested cross-talk between these domains.
Abstract
There are several factors that contribute to the specificities of protein tyrosine kinases (PTKs) in signal transduction pathways. While protein-protein interaction domains, such as the Src homology (SH2 and SH3) domains, regulate the cellular localization of PTKs and their substrates, the specificities of PTKs are ultimately determined by their catalytic domains. The use of peptide libraries has revealed the substrate specificities of SH2 domains and PTK catalytic domains, and has suggested cross-talk between these domains.
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