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Abstract
<p id="P3">Recent studies show that liquid-liquid phase separation plays a key role
in the assembly
of diverse intracellular structures. However, the biophysical principles by which
phase separation can be precisely localized within subregions of the cell are still
largely unclear, particularly for low-abundance proteins. Here we introduce an oligomerizing
biomimetic system, “Corelets”, and utilize its rapid and quantitative light-controlled
tunability to map full intracellular phase diagrams, which dictate the concentrations
at which phase separation occurs, and the mode of phase separation. Surprisingly,
both experiments and simulations show that while intracellular concentrations may
be insufficient for global phase separation, sequestering protein ligands to slowly
diffusing nucleation centers can move the cell into a different region of the phase
diagram, resulting in localized phase separation. This diffusive capture mechanism
liberates the cell from the constraints of global protein abundance and is likely
exploited to pattern condensates associated with diverse biological processes.
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