Specificity is complex and time consuming: mutual exclusivity in tyrosine kinase-mediated signaling.
Most fundamental cellular processes are transduced through tyrosine kinase (TK)-mediated pathways. 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. Stimulation of TK-mediated signals is often accompanied by recruitment of a precise, multimolecular protein complex that is itself capable of imposing specificity. Furthermore, this complex provides protection against phosphatase activity, controlling the longevity of the active signaling complex, and thus influencing outcomes in subsequent downstream events.
O'Rourke
Lisa
L
Department of Biochemistry and Molecular Biology, University College London, Gower Street, London WC1E 6BT, United Kingdom.
Ladbury
John E
JE
D000595:Amino Acid Sequence; D020935:MAP Kinase Signaling System; D046911:Macromolecular Substances; D011485:Protein Binding; D011505:Protein-Tyrosine Kinases / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D013379:Substrate Specificity; D013816:Thermodynamics
D046911:Macromolecular Substances; D011505:Protein-Tyrosine Kinases