Table 1.
Posttranslational modifications of Drp1 in cardiomyocytes/hearts.
| Type of modification | Position | Upstream molecules | Effects |
|---|---|---|---|
| Phosphorylation | S616 | CDK1/cyclin B | Phosphorylation |
| PKCδ | →Mitochondrial fragmentation | ||
| ERK1/2 | |||
| CaMKII | DePhosphorylation | ||
| ROCK | →Mitochondrial elongation | ||
| RIP1 | |||
| Phosphorylation | S637 | PKA | The specific role of S637 phosphorylation results from diverse internal and external parameters |
| PKD | |||
| Pim-1 | |||
| CaN | |||
| SUMOylation | K532, K535, | MAPL | SUMOylation |
| K594, K608, | SENP2 | →OMM translocation of Drp1, increased mitochondrial fission | |
| K606, K558, K568 | SENP3 | ||
| K597 | SENP5 | deSUMOylation | |
| →Repressed mitochondrial fission | |||
| Palmitoylation | / | ZDHHC13 | Palmitoylation |
| →Proper subcellular localization and normal function of Drp1 | |||
| Depalmitoylation | |||
| →Impaired OMM translocation of Drp1, disrupted mitochondrial dynamics | |||
| Ubiquitination | / | Parkin | Ubiquitination |
| MARCH5 | →Drp1 proteasomal degradation, enlarged and swollen mitochondria | ||
| Deubiquitination | |||
| →Decreased Drp1 degradation, excessive mitochondrial division |