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© 2021 Lee KY. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License. Mitochondria are key cellular organelles executing diverse fundamental functions, including energy conversion, calcium homeostasis, immunity and cell death. These roles are intricately regulated by changes in the structural morphology of the mitochondria1. These changes include mitochondrial fusion and fission that are controlled by the multidomain GTPase dynaminrelated proteins (DRPs): mitofusin 1/2 (Mfn1/2), optic atrophy 1 (Opa1) and dynamin-related proteins 1 (Drp1)1. Mfn1/2 and Opa1 promote fusion of adjacent mitochondria while Drp1 stimulates fission. Mfn1/2 is required for the initial tethering of fusing mitochondria2, 3. Physical interaction of Mfn1/2 with Opa1, which is stabilized by an assembly of OPA1 in the intermembrane space (IMS)4, then allows mitochondrial fusion. Conversely, Drp1 causes fission by forming distinct spiral structures on the mitochondrial outer membrane1. Mitochondrial fission is also regulated by posttranslational modification of Drp1. Phosphorylation of Drp1 at serine 616 (Ser616) by extracellular signal-regulated kinase 2 (Erk2) promotes fission5 while phosphorylation at serine 637 (Ser637) by protein kinase A (PKA) inhibits the process6. In addition, dephosphorylation of Drp1 at Ser637 by calcineurin stimulates fission7.

Cdk5 Loss Alters Mitochondrial Cristae Organization