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The modular organization of structural domains present in GEMIN5 enables this protein to perform various functions through its interaction with distinct partners. The protein is responsible for the recognition of small nuclear (sn)RNAs through its N\u2010terminal region, and therefore for snRNP assembly. Beyond its role in spliceosome assembly, GEMIN5 regulates translation through the interaction with either RNAs or proteins. In the central region, a robust dimerization domain acts as a hub for protein\u2013protein interaction, while a non\u2010canonical RNA\u2010binding site is located towards the C\u2010terminus. Interestingly, GEMIN5 regulates the partitioning of mRNAs into polysomes, likely due to its RNA\u2010binding capacity and its ability to bind native ribosomes. Understanding the functional and structural organization of the protein has brought an increasing interest in the last years with important implications in human disease. Patients carrying <jats:italic>GEMIN5<\/jats:italic> biallelic variants suffer from neurodevelopmental delay, hypotonia, and cerebellar ataxia. This review discusses recent relevant works aimed at understanding the molecular mechanisms of GEMIN5 activity in gene expression, and also the challenges to discover new functions.<\/jats:p>","DOI":"10.1002\/wrna.70008","type":"journal-article","created":{"date-parts":[[2025,4,4]],"date-time":"2025-04-04T16:58:26Z","timestamp":1743785906000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Understanding <scp>GEMIN5<\/scp> Interactions: From Structural and Functional Insights to Selective Translation"],"prefix":"10.1002","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8432-5587","authenticated-orcid":false,"given":"Encarnacion","family":"Martinez\u2010Salas","sequence":"first","affiliation":[{"name":"Centro de Biologia Molecular Severo Ochoa CSIC\u2010UAM  Madrid 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