{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T08:00:52Z","timestamp":1793174452368,"version":"4.5.0"},"reference-count":109,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"1","license":[{"start":{"date-parts":[[2025,1,13]],"date-time":"2025-01-13T00:00:00Z","timestamp":1736726400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,1]]},"abstract":"<jats:p>\n                    GEMIN5 is a predominantly cytoplasmic multifunctional protein, known to be involved in recognizing snRNAs through its WD40 repeats domain placed at the N-terminus. A dimerization domain in the middle region acts as a hub for protein\u2013protein interaction, while a non-canonical RNA-binding site is placed towards the C-terminus. The singular organization of structural domains present in GEMIN5 enables this protein to perform multiple functions through its ability to interact with distinct partners, both RNAs and proteins. This protein exerts a different role in translation regulation depending on its physiological state, such that while GEMIN5 down-regulates global RNA translation, the C-terminal half of the protein promotes translation of its mRNA. Additionally, GEMIN5 is responsible for the preferential partitioning of mRNAs into polysomes. Besides selective translation, GEMIN5 forms part of distinct ribonucleoprotein complexes, reflecting the dynamic organization of macromolecular complexes in response to internal and external signals. In accordance with its contribution to fundamental cellular processes, recent reports described clinical loss of function mutants suggesting that GEMIN5 deficiency is detrimental to cell growth and survival. Remarkably, patients carrying\n                    <jats:italic toggle=\"yes\">GEMIN5<\/jats:italic>\n                    biallelic variants suffer from neurodevelopmental delay, hypotonia, and cerebellar ataxia. Molecular analyses of individual variants, which are defective in protein dimerization, display decreased levels of ribosome association, reinforcing the involvement of the protein in translation regulation. Importantly, the number of clinical variants and the phenotypic spectrum associated with GEMIN5 disorders is increasing as the knowledge of the protein functions and the pathways linked to its activity augments. Here we discuss relevant advances concerning the functional and structural features of GEMIN5 and its separate domains in RNA-binding, protein interactome, and translation regulation, and how these data can help to understand the involvement of protein malfunction in clinical variants found in patients developing neurodevelopmental disorders.\n                  <\/jats:p>","DOI":"10.4103\/nrr.nrr-d-24-01010","type":"journal-article","created":{"date-parts":[[2025,1,17]],"date-time":"2025-01-17T05:00:16Z","timestamp":1737090016000},"page":"187-194","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":4,"title":["GEMIN5 and neurodevelopmental diseases: From functional insights to disease perception"],"prefix":"10.4103","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8432-5587","authenticated-orcid":false,"given":"Encarnacion","family":"Martinez-Salas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rosario","family":"Francisco-Velilla","sequence":"additional","affiliation":[{"name":"Genome Dynamics and Function, Centro de Biolog\u00eda Molecular Severo Ochoa, CSIC-UAM, Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","published-online":{"date-parts":[[2025,1,13]]},"reference":[{"key":"R1-20260422","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.biochi.2023.01.017","article-title":"Modular architecture and functional annotation of human RNA-binding proteins containing RNA recognition motif","volume":"209","author":"Agarwal","year":"2023","journal-title":"Biochimie"},{"key":"R2-20260422","doi-asserted-by":"crossref","first-page":"168460","DOI":"10.1016\/j.jmb.2024.168460","article-title":"Establishing order through disorder by the Hsp90 molecular chaperone","volume":"436","author":"Babu","year":"2024","journal-title":"J Mol Biol"},{"key":"R3-20260422","doi-asserted-by":"crossref","first-page":"194583","DOI":"10.1016\/j.bbagrm.2020.194583","article-title":"Cap-independent translation initiation of the unspliced RNA of retroviruses","volume":"1863","author":"Barrera","year":"2020","journal-title":"Biochim Biophys Acta Gene Regul Mech"},{"key":"R4-20260422","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1016\/j.csbj.2023.02.018","article-title":"Computational prediction of disordered binding regions","volume":"21","author":"Basu","year":"2023","journal-title":"Comput Struct Biotechnol J"},{"key":"R5-20260422","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.molcel.2006.05.036","article-title":"The Gemin5 protein of the SMN complex identifies snRNAs","volume":"23","author":"Battle","year":"2006","journal-title":"Mol Cell"},{"key":"R6-20260422","doi-asserted-by":"crossref","first-page":"27953","DOI":"10.1074\/jbc.M702317200","article-title":"SMN-independent subunits of the SMN complex. Identification of a small nuclear ribonucleoprotein assembly intermediate","volume":"282","author":"Battle","year":"2007","journal-title":"J Biol Chem"},{"key":"R7-20260422","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1016\/j.molcel.2018.10.036","article-title":"A systems-level study reveals regulators of membrane-less organelles in human cells","volume":"72","author":"Berchtold","year":"2018","journal-title":"Mol Cell"},{"key":"R8-20260422","doi-asserted-by":"crossref","first-page":"e83878","DOI":"10.1371\/journal.pone.0083878","article-title":"The Gemin associates of survival motor neuron are required for motor function in Drosophila","volume":"8","author":"Borg","year":"2013","journal-title":"PLoS One"},{"key":"R9-20260422","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.molcel.2022.12.030","article-title":"De-centralizing the central dogma: mRNA translation in space and time","volume":"83","author":"Bourke","year":"2023","journal-title":"Mol 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