Stress-induced hyperacetylation of microtubule enhances mitochondrial fission and modulates the phosphorylation of Drp1 at 616Ser.

Mitochondria dynamics results from fission and fusion events that may be unbalanced in favor of mitochondrial fragmentation upon cell stress. During oxidative stress, microtubules are hyperacetylated in a mitochondria-dependent manner. In this study, we show that under stress conditions, most of the mitochondria form foci with microtubule domains that carry Drp1. We also demonstrate that stress-induced hyperacetylation of microtubules is required for the effective induction of Drp1 phosphorylation at 616Ser, in a kinesin-1- and c-Jun N-terminal kinase-dependent manner. Furthermore, hyperacetylation of microtubules contributes to the recruitment of total Drp1 to mitochondria to enhance fission. These results highlight a new way of interaction between microtubules and mitochondria dynamics.