We sought to further unravel the reasons for dysfunctional NF-kB signalling and MyD88-recruitment and investigated by 2D gel electrophoresis combined with Immunoblot whether Mal D96N was differently posttranslationally modified compared to WT Mal. As our analysis shows, Mal WT exists as a range of species of different charge, some of which may represent differently phosphorylated species. D96N, on the other hand, showed a reduces spectrum of modification and the relative abundance of modified species was altered in comparison to WT Mal. This suggests that the D96N interferes with modification of Mal, which could potentially be linked to its defect in MyD88 trafficking. We are currently exploring the exact nature of Mal modifications and how they influence trafficking and Mal function in general.