Drp1, Mff, Fis1, and MiD51 are coordinated to mediate apopotic mitochondrial fission

What is it about?

Changes in mitochondrial morphology are tightly regulated by the balanced fusion and fission processes. Alterations in mitochondrial dynamics underlie various human diseases, including cancer, neurologic and cardiovascular diseases. Therefore, disclosing mitochondrial dynamics-related signaling pathways help us better understand roles of mitochondria involved in related disease and discover strategies for preventing the related diseases. Several mitochondrial outer membrane proteins, including mitochondrial fission protein 1 (Fis1), mitochondrial fission factor (Mff) and mitochondrial elongation factor 1 (MIEF1), have been reported to promote mitochondrial fission by recruiting the GTPase dynamin-related protein 1 (Drp1). However, fundamental issues remain concerning their function. Our aim was to investigate how Mff functions in mitochondrial fission and how the fission proteins are orchestrated to mediate fission process during apoptosis.

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Why is it important?

In the present study, we demonstrate for the first time that Mff regulates mitochondrial fission via increasing Drp1’s GTP-binding activity without affecting the oligomerization of Drp1, and the phosphorylation status of Drp1-Ser637 is critical for its interaction with Mff.

Perspectives