Abstract
The reversible postranslational modification of proteins is a ubiquitous feature of cellular signal transduction networks. In these systems, signalling is typically seen as resulting from the interaction between an active enzyme and a downstream unmodified substrate. However, it is known that in some cases the inactive form of an enzyme is also capable of binding the unmodified substrate, and that in other cases the active enzyme is capable of binding modified substrate. In this paper, we analyse the behaviour of a two-stage enzymatic cascade in which these additional protein-protein interactions are possible. Without the additional interactions, the model produces the standard ultrasensitive switch-like behaviour. We find that inactive enzyme binding to unmodified substrate increases the ultrasensitivity of this switch, while active enzyme binding to modified substrate results in the switch becoming biphasic. These results indicate how important the rules governing the occurrence of protein-protein interactions can be in determining the signalling behaviour of a pathway, even when particular protein-protein interactions have no clear functional role.
Keywords
- kinase signalling
- ultrasensitivity
- biphasic
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Seaton, D.D., Krishnan, J. (2012). Multispecific Interactions in Enzymatic Signalling Cascades. In: Lones, M.A., Smith, S.L., Teichmann, S., Naef, F., Walker, J.A., Trefzer, M.A. (eds) Information Processign in Cells and Tissues. IPCAT 2012. Lecture Notes in Computer Science, vol 7223. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-28792-3_10
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DOI: https://doi.org/10.1007/978-3-642-28792-3_10
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-28791-6
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