Discovery of the membrane receptor for mitochondrial fission GTPase Drp1

Mitochondria frequently change their morphology by fusion and fission, and these dynamic morphologic changes are essential for maintaining both mitochondrial and cellular functions. The cytoplasmic dynamin-related guanosine triphosphatase (GTPase) Drp1 (Dnm1 in yeast) is recruited to mitochondrial fission sites and severs mitochondria. Although the mitochondrial outer membrane (MOM) protein Fis1 functions as a membrane receptor for Dnm1 in yeast, it is not yet known whether the human homolog of yeast Fis1 (hFis1) is a membrane receptor for Drp1 in mammals. We recently identified the C-tail anchored MOM protein Mff as the bona fide receptor essential for recruiting Drp1 to mitochondrial fission sites. Here, we focus on this key molecule for mitochondrial fission after a brief description of the proteins involved in mitochondrial fission and fusion reactions. Finally, we discuss the expected role of hFis1 for regulating the mitochondrial dynamics in mammals.