Kinase-phosphatase cycles drive self-sustained oscillations of protein condensates

ATP-driven kinase–phosphatase cycling drives self-sustained oscillations in TDP-43 low complexity domain condensates, with condensates repeatedly appearing and disappearing under constant chemical driving.

• Why it matters: Condensates can dissolve when ATP-dependent reactions alter their physical state, but how opposing kinase and phosphatase activities produce ongoing, autonomous dynamics is unclear.
• What they did: Using molecular simulations, the study models CK1{delta} binding and action preferentially in condensed TDP-43 LCD while calcineurin dephosphorylates mainly in the dilute phase, coupled to slow kinase redistribution.
• The result: The differential recruitment and redistribution generate oscillatory condensate formation and dissolution that persists without changing chemical driving, implying kinase–phosphatase antagonism can endow condensates with autonomous dynamics.

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