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Sm-ring assembly is cytoplasmic and dependent upon the Sm-site sequence and structural motif, ATP, and Survival motor neuron (SMN) protein complex. While RNAs other than U snRNAs were previously shown to associate with Sm proteins, whether this association follows Sm-ring assembly requirements is unknown. We systematically identified Sm-sites within the human and mouse transcriptomes and assessed whether these sites can accept Sm-rings. In addition to snRNAs, Sm-sites are highly prevalent in the 3\u2032 untranslated regions of long mRNAs. RNA immunoprecipitation experiments confirm that Sm-site containing mRNAs associate with Sm proteins in the cytoplasm. In modified Sm-ring assembly assays, Sm-site containing mRNAs, specifically associate with Sm proteins in an Sm-site, SMN, and ATP-dependent manner. In cell and animal models of Spinal Muscular Atrophy (SMA), mRNAs containing Sm-sites are downregulated, suggesting reduced Sm-ring assembly on these mRNAs may contribute to SMA pathogenesis. Together, this study establishes that Sm-site containing mRNAs can accept Sm-rings and identifies a novel mechanism for Sm proteins in regulation of cytoplasmic mRNAs.<\/jats:p>","DOI":"10.1093\/nar\/gkaf794","type":"journal-article","created":{"date-parts":[[2025,8,2]],"date-time":"2025-08-02T11:42:05Z","timestamp":1754134925000},"source":"Crossref","is-referenced-by-count":0,"title":["Sm-site containing mRNAs can accept Sm-rings and are downregulated in Spinal Muscular Atrophy"],"prefix":"10.1093","volume":"53","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3557-9011","authenticated-orcid":false,"suffix":"III","given":"Anton J","family":"Blatnik","sequence":"first","affiliation":[{"name":"The Ohio State University Wexner Medical Center Department of Biological Chemistry and Pharmacology, , 395 W. 12th Ave , Columbus ,\u00a0 OH\u00a043210 ,\u00a0","place":["United 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