compared to both the control and preconditioning groups (Fig 2A). Intriguingly, in contrast to our finding in neurons, where mitochondrial partitioning of Drp1 decreases during ischaemia, in cardiac tissue we observed recruitment of Drp1 to mito-chondria, with no change in total protein levels. Furthermore, Drp1 recruitment to mitochondria was increased by precondi-tioning. In the I/R group, in which cells are undergoing apop-tosis, levels of Drp1 at the mitochondria are similar to controls (Fig 2B). Abstract 229 Figure 2 Conclusion Taken together our data suggest a delicate balance between SUMOylation and deSUMOylation that regulates the recruitment of Drp1 to mitochondria. This pathway plays an important role in the vulnerability of cardiomyocytes to ischaemic damage and myocardial reperfusion injury. Interestingly , the interplay between the relevant proteins appears to differ between heart and brain cells.

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