Drp1 catalyzes mitochondrial division, but the mechanisms remain elusive. The mitochondrial lipid cardiolipin stimulates Drp1 activity and supports membrane constriction. In addition, Drp1 populates two polymeric states that equilibrate via a dimeric intermediate. Dimers nucleate Drp1 reassembly on mitochondria for fission.
The isolated dynamin PH domain is an assembly-independent sensor of membrane curvature but not a curvature generator. In full-length dynamin, the PH alternates between two different orientations on the membrane surface during the GTP hydrolysis cycle, causing dramatic fluctuations in the diameter of dynamin polymers.
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