Analysis of the GFP-labelled β-dystroglycan interactome in Hek-293 transfected cells reveals novel intracellular networks

So far very little is known about the fine regulation of some of these intracellular interactions of β-DG and how they are perturbed in diseases. To start filling this gap, HEK-293 cells were transiently transfected with a plasmid carrying the β-DG subunit with GFP fused at its C-terminus. Immunoprecipitation by anti-GFP antibodies followed by shotgun proteomic analysis to investigate the proteins exclusively matching for β-DG binding, applying the following filters to MS identification data: high confidence, peptide rank 1, peptide length minimum 9 amino acid residues and selecting 2 peptides per protein. A series of already known β-DG interactors have been found, whilst significant new matches, which include potential novel β-DG interactors and their related networks, were identified in diverse subcellular compartments.