Abstract
The signal transduction machinery of eukaryotes is driven by changes in protein—protein associations. We have traditionally thought of signal transmission as being mediated by the altered activities of enzymes such as kinases and GTPases; in most cases, however, such changes in enzymatic activity are the result of changes in protein—protein binding. Furthermore, the activation of enzymes involved in signaling often leads in turn to further changes in their binding interactions or those of their substrates. The central importance of protein—protein binding is reinforced by the realization that most enzymes involved in signaling pathways consist of multiple protein-interaction domains (and, in some cases, lipid interaction domains) in addition to the catalytic domain itself. This modular design allows the activity of the enzyme and its local concentration relative to potential activators and substrates to be regulated by interactions with other proteins.
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Mayer, B.J. (2000). Using Protein-Interaction Domains to Manipulate Signaling Pathways. In: Gutkind, J.S. (eds) Signaling Networks and Cell Cycle Control. Cancer Drug Discovery and Development. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-218-0_24
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DOI: https://doi.org/10.1007/978-1-59259-218-0_24
Publisher Name: Humana Press, Totowa, NJ
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