Scaffold proteins play an important role in the promotion of signal trans-mission and specificity during cell signaling. In cells, signaling proteins that make up a pathway are often physically orgnaized into complexes by scaffold proteins [1]. Previous work [2] has shown that spatial localization of scaffold can enhance signaling locally while simultaneously suppressing signaling at a distance, and the membrane confinement of scaf-fold proteins may result in a precipitous spatial gradient of the active product protein, high close to the membrane and low within the cell. However, cell-fate decisions critically depend on the temporal pattern of product protein close to the nucleus. In this paper, when phosphorylation signals cannot be transfered by diffusion only, two mechanisms have been proposed for long-range signaling within cells: multiple locations of scaffold proteins and dynamical movement of scaffold proteins. Thus, here we have unveiled how the spatial propagation of the phosphorylated product protein within a cell depends on the spatially and temporal localized scaffold proteins. A class of novel and fast numerical methods for solving stiff reaction diffusion equations with complex domains is briefly introduced.
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