![]() ![]() Different scaffold levels and types might then confer specialized properties to tune evolutionarily conserved signaling modules to specific cellular contexts.Īt least one property of a MAPK cascade that permits its consideration as a separate module in the signal transduction pathway is the existence of scaffold proteins ( 4– 6). This effect and the alteration of threshold properties of the signal propagation at high scaffold concentrations might alter local signaling properties at different subcellular compartments. The location of the optimum is determined by the concentrations of the kinases rather than their binding constants and in this way is scaffold independent. In particular, for any generic scaffold there exists a concentration value optimal for signal amplitude. Analysis of this model reveals that formation of scaffold–kinase complexes can be used effectively to regulate the specificity, efficiency, and amplitude of signal propagation. Here we describe a quantitative computer model of MAPK cascade with a generic scaffold protein. To date, however, no detailed biochemical model of scaffold action has been suggested. In many cases, such as mitogen-activated protein kinase (MAPK) cascades, scaffold proteins are necessary for full activation of a signaling pathway. In addition to preventing crosstalk among related signaling pathways, scaffold proteins might facilitate signal transduction by preforming multimolecular complexes that can be rapidly activated by incoming signal. ![]()
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