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Significance The large cytosolic GTPase dynamin-related protein 1 (Drp1) self-assembles around mitochondria to mechanoenzymatically constrict and divide the double-membrane–bound organelle. Although Drp1 recruitment to the mitochondrial surface is contingent upon its binding to protein adaptors, subsequent or coincident interactions with the outer membrane–localized, mitochondria-specific phospholipid cardiolipin (CL) is critical for stress-induced mitochondrial fission. Here, using a combination of multimodal NMR spectroscopy and various biophysical, biochemical, and cellular approaches, we show the intrinsically disordered variable domain of Drp1 undergoes an ordered helical structural transition to penetrate the membrane bilayer and selectively bind CL. The mutation of key residues within an identified CL-binding motif (CBM) results in defective mitochondrial division coupled to the formation of morphologically distinct “donut” mitochondria.

NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission