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In multiple sclerosis (MS), myelin debris is phagocytosed by microglia (MG), and prior studies have detected myelin-derived mRNA in MG nuclei, suggesting a retrograde transport pathway. We report myelin basic protein (MBP) is a nucleic acid\u2013binding and trafficking protein. We found that retro-transport of myelin RNA into the MG nucleus was phagocytosis and importin-dependent. Transcriptomic and proteomic analyses of MG nuclei revealed enrichment of myelin mRNAs and proteins, with MBP singularly detected in soluble and chromatin-associated fractions. MBP bound mRNA with high affinity (Kd \u2248 0.30 nM) and was sufficient to facilitate MG RNA nuclear import\n                  <jats:italic>in vitro<\/jats:italic>\n                  and\n                  <jats:italic>in vivo<\/jats:italic>\n                  . Functionally, MBP mediated the delivery of small interfering RNAs for targeted knockdown of\n                  <jats:italic>toll-like receptor 4<\/jats:italic>\n                  . These findings indicate MBP as an RNA-binding protein capable of MG nuclear import, providing insight into neuroinflammatory pathology of MS.\n                <\/jats:p>","DOI":"10.64898\/2026.05.14.725089","type":"posted-content","created":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T18:45:13Z","timestamp":1778957113000},"source":"Crossref","is-referenced-by-count":0,"title":["Myelin basic protein is an RNA chaperone in microglial nuclear retro-transport"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6184-304X","authenticated-orcid":false,"given":"Guy","family":"Lam","sequence":"first","affiliation":[{"name":"Cambridge Stem Cell Institute, University of Cambridge, Puddicombe Way, Cambridge Biomedical Campus, Cambridge CB2 0AW, UK"},{"name":"Department of Paediatrics, University of Cambridge, Cambridge CB2 0QQ, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhao 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