Abstract
The review summarizes for the first time the current concepts of the role of tyrosine phosphorylation in regulation of signal transduction pathways in unicellular eukaryotes. Evolutionary concepts are developed about the origin of protein tyrosine kinases (PTK)-signaling.
Highlights
At the end of the last century, in mammalian cells a multicascade pathway was discovered to be responsible for transmission of proliferative signals into genome
Phosphorylation of tyrosine residues in proteins is catalyzed by retrovirus protein tyrosine kinases (PTKs), their cellular homologues (Bishop, 1983) or by tyrosine kinases associated with growth factor receptors (Yarden and Ullrich, 1988; Broome and Hunter, 1996)
The most intensively studied microbial Ras subfamily members activate adenylyl cyclase and are involved in Ras-protein kinase A (PKA) pathways; only in few eukaryotic microorganisms, Ras proteins are involved in Ras-MAPK signaling that have great similarity with such in mammals. This suggests that in evolution of the eukaryotic organisms the Ras proteins originally participated in regulating cAMP-dependent signal pathways and their role in the MEKK-MEK-MAPK module stimulation is connected with transition from unicellularity to multicellularity
Summary
At the end of the last century, in mammalian cells a multicascade pathway was discovered to be responsible for transmission of proliferative signals into genome. Ushiro and Cohen (1980) were the first to establish the important role of phosphorylation of tyrosine as a regulator of intracellular processes and to reveal changes of tyrosine kinase activity of proteins in mammalian cells in response to action of growth factors.
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