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The interaction between the diaphanous inhibitory domain (DID) and the diaphanous autoregulatory domain (DAD) is a key regulatory mechanism in diaphanous-related formins (DRFs). This interaction maintains DRFs in an autoinhibited state, preventing FH2-mediated actin polymerization, until activation by upstream signals like Rho GTPases. Disruption of this interaction leads to the activation of DRFs and subsequent actin polymerization, influencing cell shape, migration, division, and development. DRFs also coordinate microtubule stabilization.
Inhibition of DID-DAD interaction to activate Formins.
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