Cyanidioschyzon merolae aurora kinase phosphorylates evolutionarily conserved sites on its target to regulate mitochondrial division

• Published in: Communications biology 2019-12, Vol.2 (1), p.477
• Main Authors: Kato, Shoichi, Okamura, Erika, Matsunaga, Tomoko M, Nakayama, Minami, Kawanishi, Yuki, Ichinose, Takako, Iwane, Atsuko H, Sakamoto, Takuya, Imoto, Yuuta, Ohnuma, Mio, Nomura, Yuko, Nakagami, Hirofumi, Kuroiwa, Haruko, Kuroiwa, Tsuneyoshi, Matsunaga, Sachihiro
• Format: Article
• Language: English
• ISSN: 2399-3642
• DOI: 10.1038/s42003-019-0714-x

The mitochondrion is an organelle that was derived from an endosymbiosis. Although regulation of mitochondrial growth by the host cell is necessary for the maintenance of mitochondria, it is unclear how this regulatory mechanism was acquired. To address this, we studied the primitive unicellular red alga Cyanidioschyzon merolae, which has the simplest eukaryotic genome and a single mitochondrion. Here we show that the C. merolae Aurora kinase ortholog CmAUR regulates mitochondrial division through phosphorylation of mitochondrial division ring components. One of the components, the Drp1 ortholog CmDnm1, has at least four sites phosphorylated by CmAUR. Depletion of the phosphorylation site conserved among eukaryotes induced defects such as mitochondrial distribution on one side of the cell. Taken together with the observation that human Aurora kinase phosphorylates Drp1 in vitro, we suggest that the phosphoregulation is conserved from the simplest eukaryotes to mammals, and was acquired at the primitive stage of endosymbiosis.