As it is known that the mutated hypofunctional GNE is associated with intracellular accumulation of amyloid β-peptide (Aβ) in patient muscles (see “biopsy findings and pathophysiological studies on patient-derived muscle” section) Bosch-Morató and colleagues [49] addressed the underlying mechanism by using C2C12 cells and demonstrated that systematic reduction of sialic acid favors Aβ1-42 endocytosis in a clathrin and heparan sulfate proteoglycan-dependent manner explaining the enhanced Aβ1-42 internalization in myoblasts from a GNE myopathy patient. This evidence concerns the gene GNE and GNE myopathy.