Does Altered Membrane Glycosylation Contribute to Neurodevelopmental Dysfunction in Autism Spectrum Disorder?

Neuronal development relies on cell-surface glycoconjugates that function as complex bioinformational codes. Recently, altered glycosylation has emerged as a central mechanistic theme in the pathophysiology of autism spectrum disorder (ASD). Critically, the brain maintains a distinctively restricted glycan profile through strict biosynthetic regulation, creating a specialized landscape highly susceptible to homeostatic perturbation. This “membrane-centric vulnerability” spans both glycoproteins and glycolipids; however, evidence remains fragmented, obscuring their pathogenic interplay. To bridge this gap, this review synthesizes evidence for these two primary classes of membrane glycoconjugates into a unified framework.