| In order to cope with conditions of low oxygen, the cell can alter its metabolism to survive in the face of reduced capability for oxidative phosphorylation. Peroxisome proliferator receptor gamma coactivator-1alpha (PGC-1alpha), a master regulator of oxidative metabolism, plays a critical role in this response. Under hypoxic conditions, we show that the full-length protein, as well as a truncated form (NT-PGC-1alpha), are upregulated when subjected to a hypoxic event. Under hypoxic conditions, the main function of PGC-1alpha is as a regulator of mitochondrial biogenesis, was inhibited. Both forms of the protein have the ability to be heavily posttranslationally modified. Recent evidence has shown that SUMOylation plays a key role in regulating the proteins activity. The SUMOylation status of both forms of PGC-1alpha under hypoxia were examined. Disruption of the SUMOylation site on PGC-1alpha and NT -PGC-1alpha appeared to play differential roles amongst both forms of the protein, as well as altered the truncated form's ability to undergo further posttranslational modifications. |
