作者: Tony Hunter , Gerard Manning
DOI: 10.1007/978-1-4939-2053-2_1
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摘要: The presence of tightly bound phosphate in proteins was discovered 1883 and covalent attachment to 1906, but this important posttranslational modification had been “invented” by evolution billion years before early prokaryotes. Tyrosine phosphorylation, as distinct from serine threonine 1979 appears have arisen single-celled eukaryotes that were the antecedents first multicellular animals. Sophisticated cell-cell communication a sine qua non for emergence organisms, development cell surface receptor systems utilize tyrosine phosphorylation transmembrane signal transduction intracellular signaling seems likely crucial event metazoans. Like all types protein can regulate multiple ways, most function phosphotyrosine (P.Tyr) is serve docking site promotes specific interaction between tyrosine-phosphorylated another contains P.Tyr-binding domain, such an SH2 domain. Once kinase (RTK) activated becomes autophosphorylated upon binding extracellular ligand, P.Tyr interactions sort initiate through cytoplasmic pathways and, consequence, elicit cellular outcomes. This chapter reviews family how kinases particular, could be ligand evolved key roles transduction.