Mff oligomerization is required for Drp1 activation and synergy with actin filaments during mitochondrial division
Ao Liu, Frieda Kage, Henry N. Higgs
Abstract
in the range of 10 µM. Dynamic Mff oligomerization is required for Drp1 activation. While not binding Mff directly, actin filaments enhance Mff-mediated Drp1 activation by lowering the effective Mff concentration 10-fold. Total internal reflection microscopy assays using purified proteins show that Mff interacts with Drp1 on actin filaments in a manner dependent on Mff oligomerization. In U2OS cells, oligomerization-defective Mff does not effectively rescue three defects in Mff knockout cells: mitochondrial division, mitochondrial Drp1 recruitment, and peroxisome division. The ability of Mff to assemble into puncta on mitochondria depends on its oligomerization, as well as on actin filaments and Drp1.
Topics & Concepts
Cell biologyMitochondrial fissionBiologyActinMitochondrionCytosolMitochondrial apoptosis-induced channelBiophysicsInner mitochondrial membraneBiochemistryEnzymeMitochondrial Function and PathologyATP Synthase and ATPases ResearchMetabolism and Genetic Disorders