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The genesis of tyrosine phosphorylation
#MMPMID24789824
Hunter T
Cold Spring Harb Perspect Biol
2014[May]; 6
(5
): a020644
PMID24789824
show ga
Tyrosine phosphorylation of proteins was discovered in 1979, but this
posttranslational modification had been "invented" by evolution more than a
billion years ago in single-celled eukaryotic organisms that were the antecedents
of the first multicellular animals. Because sophisticated cell-cell communication
is a sine qua non for the existence of multicellular organisms, the development
of cell-surface receptor systems that use tyrosine phosphorylation for
transmembrane signal transduction and intracellular signaling seems likely to
have been a crucial event in the evolution of metazoans. Like all types of
protein phosphorylation, tyrosine phosphorylation serves to regulate proteins in
multiple ways, including causing electrostatic repulsion and inducing allosteric
transitions, but the most important function of phosphotyrosine (P.Tyr) is to
serve as a docking site that promotes a specific interaction between a tyrosine
phosphorylated protein and another protein that contains a P.Tyr-binding domain,
such as an SH2 or PTB domain. Such docking interactions are essential for signal
transduction downstream from receptor tyrosine kinases (RTKs) on the cell
surface, which are activated on binding a cognate extracellular ligand, and, as a
consequence, elicit specific cellular outcomes.
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