Format

Send to

Choose Destination
Commun Biol. 2019 Dec 20;2:477. doi: 10.1038/s42003-019-0714-x. eCollection 2019.

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

Author information

1
1Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510 Japan.
2
2Research Institute for Science and Technology, Tokyo University of Science, Noda, Chiba 278-8510 Japan.
3
RIKEN Center for Biosystems Dynamics Research, 3-10-23 Kagamiyama, Higashi-Hiroshima, Hiroshima 739-0046 Japan.
4
4Department of Cell Biology, Johns Hopkins University School of Medicine, 725N. Wolfe Street, 100 Biophysics, Baltimore, MD 21205 USA.
5
5National Institute of Technology, Hiroshima College, Hiroshima, 725-0231 Japan.
6
RIKEN CSRS, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045 Japan.
7
7Protein Mass Spectrometry Group, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, 50829 Cologne, Germany.
8
8Department of Chemical and Biological Science, Japan Women's University, Tokyo, 112-8681 Japan.

Abstract

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.

KEYWORDS:

Cell biology; Plant sciences

Conflict of interest statement

Competing interestsThe authors declare no competing interests.

Supplemental Content

Full text links

Icon for PubMed Central
Loading ...
Support Center