α-DG glycosylation pattern is considered crucial for its function in terms of laminin binding affinity, and a disruption of the α-DG/laminin network is at the basis of a group of diseases spanning from the severe congenital to the much milder limb-girdle muscular dystrophies, defined as secondary dystroglycanopathies [1]. Here, LAMB2 is linked to neuromuscular disease caused by qualitative or quantitative defects of alpha-dystroglycan.