Optimal control of protein copy number

Cell-cell communication is often achieved by secreted signaling molecules that bind membrane-bound receptors. A common class of such receptors are G-protein coupled receptors, where extracellular binding induces changes on the membrane affinity near the receptor for certain cytosolic proteins, effectively altering their chemical potential. We analyze the minimum-dissipation schedules for dynamically changing chemical potential to induce steady-state changes in protein copy-number distributions, and illustrate with analytic solutions for linear chemical reaction networks. Protocols that change chemical potential on biologically relevant timescales are experimentally accessible using optogenetic manipulations, and our framework provides nontrivial predictions about functional dynamical cell-cell interactions.