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Drp1 is a dynamin-like GTPase that mediates mitochondrial and peroxisomal division in a process dependent on self-assembly and coupled to GTP hydrolysis. Despite the link between Drp1 malfunction and human disease, the molecular details of its membrane activity remain poorly understood.
Another dynamin-related protein, Drp1, which localizes primarily in the cytoplasm, is involved in mitochondrial fission, probably in cooperation with the outer-membrane proteins Fis1 (refs 1, 2, 3) and Mff4.
Mitochondrial dynamics is mainly regulated by a number of GTPase family proteins. While MFN1/2 and OPA1 are responsible for the fusion process, dynamin-like protein 1 (Drp1) regulates mitochondrial fission along with its adaptors proteins such as Fis1 and Mff [3, 4]. Drp1 is located mainly in the cytosol.
Drp1 mediates fission of the outer mitochondrial membrane that sequesters cytochrome c and other apoptogenic proteins from the cytosol in healthy cells.
Drp1 binds to mitochondrial adaptors, assembles future fission sites, and severs mitochondrial membrane in a GTP hydrolysis-dependent manner [6]. The activation of Drp1 is regulated by posttranslational modification, among which phosphorylation of Drp1 can either inhibit or activate its enzymatic activity.

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In mammalian cells, Drp1 primarily resides in the cytosol, but can be recruited to mitochondria through its mitochondrial receptors, Mff and MIEFs (MIEF1/MiD51 and MIEF2/MiD49), which are anchored in the mitochondrial outer membrane (Otera et al., 2010; Palmer et al., 2011; Zhao et al., 2011; Liu et al., 2013; Yu et al ...
The classic role of mitochondria is oxidative phosphorylation, which generates ATP by utilizing the energy released during the oxidation of the food we eat. ATP is used in turn as the primary energy source for most biochemical and physiological processes, such as growth, movement and homeostasis.
Drp1 mediates fission of the outer mitochondrial membrane that sequesters cytochrome c and other apoptogenic proteins from the cytosol in healthy cells.
Residing in the cytosol as dimers and tetramers, Drp1 is recruited by receptors on the mitochondrial outer membrane, where it further assembles into a helical ring that drives division via GTP-dependent constriction.
Further constriction of mitochondria is driven by dynamin-related protein 1 (Drp1), a mechanochemical enzyme encoded by the DNM1L gene (7). The protein is found in the cytosol and is recruited to mitochondria by protein receptors embedded in the mitochondrial outer membrane.

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