{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,3]],"date-time":"2026-07-03T22:10:13Z","timestamp":1783116613921,"version":"3.54.6"},"reference-count":138,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100005283","name":"Funda\u00e7\u00e3o Cearense de Apoio ao Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100005283","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Membranes"],"abstract":"<jats:p>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 \u201cmembrane-centric vulnerability\u201d 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. We examine how defects in key glycoproteins (such as NCAM1 and neuroligins) directly impair synaptic signaling, trafficking, and plasticity. We then demonstrate how these defects are functionally coupled to the glycolipid (ganglioside) environment, which organizes the lipid raft platforms essential for glycoprotein function. We propose that these two systems are not independent but represent a final common pathway for diverse etiological drivers. Genetic variants (e.g., MAN2A2), environmental factors (e.g., valproic acid), and epigenetic dysregulation (e.g., miRNAs) all converge on this mechanism of impaired glycan maturation. This model elucidates how distinct upstream causes can produce a common downstream synaptic pathology by compromising the integrity of the membrane signaling platform.<\/jats:p>","DOI":"10.3390\/membranes16010018","type":"journal-article","created":{"date-parts":[[2026,1,2]],"date-time":"2026-01-02T09:56:23Z","timestamp":1767347783000},"page":"18","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Does Altered Membrane Glycosylation Contribute to Neurodevelopmental Dysfunction in Autism Spectrum Disorder?"],"prefix":"10.3390","volume":"16","author":[{"given":"Vinicius J. S.","family":"Osterne","sequence":"first","affiliation":[{"name":"BioMol-Lab, Department of Biochemistry and Molecular Biology, Federal University of Cear\u00e1, Fortaleza 60440-970, Cear\u00e1, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4754-7743","authenticated-orcid":false,"given":"Messias V.","family":"Oliveira","sequence":"additional","affiliation":[{"name":"BioMol-Lab, Department of Biochemistry and Molecular Biology, Federal University of Cear\u00e1, Fortaleza 60440-970, Cear\u00e1, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vanir R.","family":"Pinto-Junior","sequence":"additional","affiliation":[{"name":"BioMol-Lab, Department of Biochemistry and Molecular Biology, Federal University of Cear\u00e1, Fortaleza 60440-970, Cear\u00e1, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francisco S. B.","family":"Mota","sequence":"additional","affiliation":[{"name":"IPREDE\u2014Instituto da Primeira Inf\u00e2ncia, Fortaleza 60821-728, Cear\u00e1, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5791-6170","authenticated-orcid":false,"given":"Benildo S.","family":"Cavada","sequence":"additional","affiliation":[{"name":"BioMol-Lab, Department of Biochemistry and Molecular Biology, Federal University of Cear\u00e1, Fortaleza 60440-970, Cear\u00e1, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyria S.","family":"Nascimento","sequence":"additional","affiliation":[{"name":"BioMol-Lab, Department of Biochemistry and Molecular Biology, Federal University of Cear\u00e1, Fortaleza 60440-970, Cear\u00e1, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,1,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"57R","DOI":"10.1093\/glycob\/cwm018","article-title":"The Expression and Functions of Glycoconjugates in Neural Stem Cells","volume":"17","author":"Yanagisawa","year":"2007","journal-title":"Glycobiology"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1007\/978-1-4939-1154-7_9","article-title":"Glycolipid and Glycoprotein Expression during Neural Development","volume":"9","author":"Yu","year":"2014","journal-title":"Adv. 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