Figure 6.

Phosphorylation-driven modulation of membrane association allows tyrosines to operate as a regulatory switch yet still remain accessible in the “off” state. Average binding rates of (A) kinase and (B) phosphatase binding to ɛ at different (de)phosphorylation states for varying strengths of phosphorylated tyrosine potential (E_P0) are shown (blue: weak; yellow: strong). Both kinase and phosphatase are assumed to have a radius of 2.1 nm. Rates are normalized to the free-space binding rate. To see this figure in color, go online.