O00429

DRP1 also known as Dynamin-like protein 1, Dlp1, DVLP, DNM1L is a member of the dynamin superfamily of GTPases. DRP1 plays a crucial role in mediating outer mitochondrial membrane fission in mammalian cells, a process essential for mitochondrial dynamics and cellular health. DRP1 is characterized by an N-terminal tripartite GTP-binding domain, which is a hallmark of the Dynamin superfamily of GTPases. Structurally, DRP1 exists as a T-shaped dimer composed of a head, leg, and stalk, and GTP binding induces a conformational change that generates the mechanical force necessary for membrane constriction. DRP1 is ubiquitously expressed, with particularly high levels in skeletal muscle, heart, kidney, and brain tissues, and localizes to the perinuclear region within cells. In mouse brain, DRP1 shows high expression in the cerebellum, especially in Purkinje cells, highlighting DRP1′s importance in neuronal function. During apoptosis, DRP1 translocates from the cytosol to mitochondria, localizing to sites of organe.