(A) At the microscopic scale, interactions between the terminal extensions and hinge domain toggles HP1α between autoinhibited and active states. DNA biases HP1α to the active state. (B) At the intermediate scale, HP1α and DNA cluster into proto-condensates. (C) If HP1α is present above the critical concentration, proto-condensates aggregate into large macroscopic droplets characterized by liquid behavior of HP1α and static DNA held in sub-condensate domains. (D) At genomic loci, HP1α condensates are remodeled by forces, resisting and strengthening in response to instantaneous forces, but relaxing and weakening in response to sustained forces. HP1α domains are also subject to disruption and reinforcement from HP1-interacting proteins like HP1β.