{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T15:33:46Z","timestamp":1790696026051,"version":"4.1.0"},"reference-count":102,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2020,5,29]],"date-time":"2020-05-29T00:00:00Z","timestamp":1590710400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003329","name":"Ministerio de Economia y Competitividad","doi-asserted-by":"publisher","award":["BFU2017-84492-R"],"award-info":[{"award-number":["BFU2017-84492-R"]}],"id":[{"id":"10.13039\/501100003329","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012818","name":"Comunidad de Madrid","doi-asserted-by":"publisher","award":["B2017\/BMD-3770"],"award-info":[{"award-number":["B2017\/BMD-3770"]}],"id":[{"id":"10.13039\/100012818","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>RNA-binding proteins (RBPs) play a pivotal role in the lifespan of RNAs. The disfunction of RBPs is frequently the cause of cell disorders which are incompatible with life. Furthermore, the ordered assembly of RBPs and RNAs in ribonucleoprotein (RNP) particles determines the function of biological complexes, as illustrated by the survival of the motor neuron (SMN) complex. Defects in the SMN complex assembly causes spinal muscular atrophy (SMA), an infant invalidating disease. This multi-subunit chaperone controls the assembly of small nuclear ribonucleoproteins (snRNPs), which are the critical components of the splicing machinery. However, the functional and structural characterization of individual members of the SMN complex, such as SMN, Gemin3, and Gemin5, have accumulated evidence for the additional roles of these proteins, unveiling their participation in other RNA-mediated events. In particular, Gemin5 is a multidomain protein that comprises tryptophan-aspartic acid (WD) repeat motifs at the N-terminal region, a dimerization domain at the middle region, and a non-canonical RNA-binding domain at the C-terminal end of the protein. Beyond small nuclear RNA (snRNA) recognition, Gemin5 interacts with a selective group of mRNA targets in the cell environment and plays a key role in reprogramming translation depending on the RNA partner and the cellular conditions. Here, we review recent studies on the SMN complex, with emphasis on the individual components regarding their involvement in cellular processes critical for cell survival.<\/jats:p>","DOI":"10.3390\/ijms21113868","type":"journal-article","created":{"date-parts":[[2020,6,2]],"date-time":"2020-06-02T04:09:03Z","timestamp":1591070943000},"page":"3868","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":43,"title":["Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control"],"prefix":"10.3390","volume":"21","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8432-5587","authenticated-orcid":false,"given":"Encarnacion","family":"Martinez-Salas","sequence":"first","affiliation":[{"name":"Centro de Biolog\u00eda Molecular Severo Ochoa, CSIC-UAM, Nicol\u00e1s Cabrera 1, 28049 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1980-942X","authenticated-orcid":false,"given":"Azman","family":"Embarc-Buh","sequence":"additional","affiliation":[{"name":"Centro de Biolog\u00eda Molecular Severo Ochoa, CSIC-UAM, Nicol\u00e1s Cabrera 1, 28049 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4328-8732","authenticated-orcid":false,"given":"Rosario","family":"Francisco-Velilla","sequence":"additional","affiliation":[{"name":"Centro de Biolog\u00eda Molecular Severo Ochoa, CSIC-UAM, Nicol\u00e1s Cabrera 1, 28049 Madrid, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,5,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.tibs.2017.02.004","article-title":"Deciphering the mRNP Code: RNA-Bound Determinants of Post-Transcriptional Gene Regulation","volume":"42","author":"Gehring","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"3745","DOI":"10.1038\/emboj.2012.220","article-title":"DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs","volume":"31","author":"Rubilar","year":"2012","journal-title":"EMBO J."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1128\/MCB.06177-11","article-title":"Rhythmic interaction between Period1 mRNA and hnRNP Q leads to circadian time-dependent translation","volume":"32","author":"Lee","year":"2012","journal-title":"Mol. Cell Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1146\/annurev-biochem-060713-035802","article-title":"The scanning mechanism of eukaryotic translation initiation","volume":"83","author":"Hinnebusch","year":"2014","journal-title":"Annu. Rev. Biochem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/nrmicro2655","article-title":"Viral subversion of the host protein synthesis machinery","volume":"9","author":"Walsh","year":"2011","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"180155","DOI":"10.1098\/rsob.180155","article-title":"Deconstructing internal ribosome entry site elements: An update of structural motifs and functional divergences","volume":"8","author":"Lozano","year":"2018","journal-title":"Open Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/j.tibs.2017.06.002","article-title":"Ribosomal Chamber Music: Toward an Understanding of IRES. Mechanisms","volume":"42","author":"Yamamoto","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.sbi.2009.03.005","article-title":"Toward a structural understanding of IRES. RNA function","volume":"19","author":"Filbin","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.coviro.2015.04.008","article-title":"Structural insights into viral IRES-dependent translation mechanisms","volume":"12","author":"Lozano","year":"2015","journal-title":"Curr. Opin. Virol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1038\/334320a0","article-title":"Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA","volume":"334","author":"Pelletier","year":"1988","journal-title":"Nature"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2636","DOI":"10.1128\/jvi.62.8.2636-2643.1988","article-title":"A segment of the 5\u2032 nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation","volume":"62","author":"Jang","year":"1988","journal-title":"J. Virol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"5545","DOI":"10.1038\/s41598-018-23845-x","article-title":"Ribosome-dependent conformational flexibility changes and RNA dynamics of IRES domains revealed by differential SHAPE","volume":"8","author":"Lozano","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"594","DOI":"10.3389\/fmicb.2015.00594","article-title":"Picornaviruses and nuclear functions: Targeting a cellular compartment distinct from the replication site of a positive-strand RNA virus","volume":"6","author":"Flather","year":"2015","journal-title":"Front. Microbiol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.tim.2017.01.010","article-title":"Regulation Mechanisms of Viral IRES-Driven Translation","volume":"25","author":"Lee","year":"2017","journal-title":"Trends Microbiol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/S0092-8674(00)00055-6","article-title":"Initiation of protein synthesis from the A site of the ribosome","volume":"102","author":"Wilson","year":"2000","journal-title":"Cell"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.cell.2014.04.015","article-title":"Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome","volume":"157","author":"Fernandez","year":"2014","journal-title":"Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.neuron.2019.03.014","article-title":"Disruption of RNA Metabolism in Neurological Diseases and Emerging Therapeutic Interventions","volume":"102","author":"Nussbacher","year":"2019","journal-title":"Neuron"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/nrn2670","article-title":"Spinal muscular atrophy: Why do low levels of survival motor neuron protein make motor neurons sick?","volume":"10","author":"Burghes","year":"2009","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"5825","DOI":"10.1074\/jbc.M608528200","article-title":"A comprehensive interaction map of the human survival of motor neuron (SMN) complex","volume":"282","author":"Otter","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/nsmb.1584","article-title":"Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains","volume":"16","author":"Lau","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1038\/ncb1101-945","article-title":"A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs","volume":"3","author":"Meister","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/S0955-0674(00)00211-8","article-title":"Spliceosomal UsnRNP biogenesis, structure and function","volume":"13","author":"Will","year":"2001","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3103","DOI":"10.1016\/j.celrep.2016.08.047","article-title":"The Ribosome Cooperates with the Assembly Chaperone pICln to Initiate Formation of snRNPs","volume":"16","author":"Paknia","year":"2016","journal-title":"Cell Rep."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.cell.2008.09.020","article-title":"An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs","volume":"135","author":"Chari","year":"2008","journal-title":"Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.1016\/j.str.2012.08.024","article-title":"The survival motor neuron protein forms soluble glycine zipper oligomers","volume":"20","author":"Martin","year":"2012","journal-title":"Structure"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1091\/mbc.E17-11-0627","article-title":"Self-oligomerization regulates stability of survival motor neuron protein isoforms by sequestering an SCF(Slmb) degron","volume":"29","author":"Gray","year":"2018","journal-title":"Mol. Biol. Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"20185","DOI":"10.1074\/jbc.M115.667279","article-title":"Oligomeric Properties of Survival Motor Neuron.Gemin2 Complexes","volume":"290","author":"Gupta","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1038\/83014","article-title":"SMN tudor domain structure and its interaction with the Sm proteins","volume":"8","author":"Selenko","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1016\/j.cell.2011.06.043","article-title":"Structure of a key intermediate of the SMN complex reveals Gemin2\u2032s crucial function in snRNP assembly","volume":"146","author":"Zhang","year":"2011","journal-title":"Cell"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.ejcb.2014.01.006","article-title":"Phosphoregulation of the human SMN complex","volume":"93","author":"Husedzinovic","year":"2014","journal-title":"Eur. J. Cell Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.molcel.2010.03.014","article-title":"Gemin5 delivers snRNA precursors to the SMN complex for snRNP biogenesis","volume":"38","author":"Yong","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_32","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":"ref_33","doi-asserted-by":"crossref","first-page":"10045","DOI":"10.1073\/pnas.0802287105","article-title":"Evolution of an RNP assembly system: A minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster","volume":"105","author":"Kroiss","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1083\/jcb.147.6.1181","article-title":"Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems","volume":"147","author":"Charroux","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"bio032409","DOI":"10.1242\/bio.032409","article-title":"Gemin4 is an essential gene in mice, and its overexpression in human cells causes relocalization of the SMN complex to the nucleoplasm","volume":"7","author":"Meier","year":"2018","journal-title":"Biol. Open"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1016\/j.str.2005.03.014","article-title":"The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex has an Sm protein-like structure","volume":"13","author":"Ma","year":"2005","journal-title":"Structure"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"37009","DOI":"10.1074\/jbc.M607505200","article-title":"Gemin8 is required for the architecture and function of the survival motor neuron complex","volume":"281","author":"Carissimi","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"17372","DOI":"10.1073\/pnas.0508947102","article-title":"Gemin proteins are required for efficient assembly of Sm-class ribonucleoproteins","volume":"102","author":"Shpargel","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"10126","DOI":"10.1073\/pnas.152318699","article-title":"Gene targeting of Gemin2 in mice reveals a correlation between defects in the biogenesis of U snRNPs and motoneuron cell death","volume":"99","author":"Jablonka","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1093\/hmg\/ddi168","article-title":"Gemins modulate the expression and activity of the SMN complex","volume":"14","author":"Feng","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1091\/mbc.e08-01-0024","article-title":"Gemin3 is an essential gene required for larval motor function and pupation in Drosophila","volume":"20","author":"Shpargel","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.nbd.2016.06.015","article-title":"Disruption of snRNP biogenesis factors Tgs1 and pICln induces phenotypes that mirror aspects of SMN-Gemins complex perturbation in Drosophila, providing new insights into spinal muscular atrophy","volume":"94","author":"Borg","year":"2016","journal-title":"NeuroBiol. Dis."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1242\/dev.00920","article-title":"rigor mortis encodes a novel nuclear receptor interacting protein required for ecdysone signaling during Drosophila larval development","volume":"131","author":"Gates","year":"2004","journal-title":"Development"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Cauchi, R.J., Davies, K.E., and Liu, J.L. (2008). A motor function for the DEAD-box RNA helicase, Gemin3, in Drosophila. PLoS Genet., 4.","DOI":"10.1371\/journal.pgen.1000265"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Borg, R.M., Bordonne, R., Vassallo, N., and Cauchi, R.J. (2015). Genetic Interactions between the Members of the SMN-Gemins Complex in Drosophila. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0130974"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2835","DOI":"10.1016\/j.yexcr.2011.09.001","article-title":"U bodies respond to nutrient stress in Drosophila","volume":"317","author":"Buckingham","year":"2011","journal-title":"Exp. Cell Res."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1038\/sj.embor.7400301","article-title":"Phosphorylation regulates the activity of the SMN complex during assembly of spliceosomal U snRNPs","volume":"6","author":"Grimmler","year":"2005","journal-title":"EMBO Rep."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1016\/j.celrep.2017.01.059","article-title":"The Survival of Motor Neuron Protein Acts as a Molecular Chaperone for mRNP Assembly","volume":"18","author":"Fallini","year":"2017","journal-title":"Cell Rep."},{"key":"ref_49","first-page":"10983","article-title":"High-affinity RNA targets of the Survival Motor Neuron protein reveal diverse preferences for sequence and structural motifs","volume":"46","author":"Ottesen","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3811","DOI":"10.1523\/JNEUROSCI.2396-15.2016","article-title":"Deficiency of the Survival of Motor Neuron Protein Impairs mRNA Localization and Local Translation in the Growth Cone of Motor Neurons","volume":"36","author":"Fallini","year":"2016","journal-title":"J. Neurosci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1261\/rna.056788.116","article-title":"A new cis-acting motif is required for the axonal SMN-dependent Anxa2 mRNA localization","volume":"23","author":"Rihan","year":"2017","journal-title":"RNA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1093\/hmg\/dds474","article-title":"A novel function for the survival motoneuron protein as a translational regulator","volume":"22","author":"Sanchez","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"3159","DOI":"10.1093\/hmg\/ddq226","article-title":"PTEN depletion rescues axonal growth defect and improves survival in SMN-deficient motor neurons","volume":"19","author":"Ning","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.nmd.2010.06.010","article-title":"Ultrastructural changes in diaphragm neuromuscular junctions in a severe mouse model for Spinal Muscular Atrophy and their prevention by bifunctional U7 snRNA correcting SMN2 splicing","volume":"20","author":"Voigt","year":"2010","journal-title":"Neuromuscul. Disord."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1083\/jcb.200610053","article-title":"A Drosophila melanogaster model of spinal muscular atrophy reveals a function for SMN in striated muscle","volume":"176","author":"Rajendra","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"5443","DOI":"10.1093\/emboj\/20.19.5443","article-title":"SMN interacts with a novel family of hnRNP and spliceosomal proteins","volume":"20","author":"Mourelatos","year":"2001","journal-title":"EMBO J."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1101\/gad.974702","article-title":"miRNPs: A novel class of ribonucleoproteins containing numerous microRNAs","volume":"16","author":"Mourelatos","year":"2002","journal-title":"Genes Dev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1016\/j.molcel.2012.12.009","article-title":"Structural basis of assembly chaperone- mediated snRNP formation","volume":"49","author":"Grimm","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1534\/g3.118.200874","article-title":"Composition of the Survival Motor Neuron (SMN) Complex in Drosophila melanogaster","volume":"9","author":"Matera","year":"2019","journal-title":"G3 (Bethesda)"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1038\/nature13302","article-title":"A draft map of the human proteome","volume":"509","author":"Kim","year":"2014","journal-title":"Nature"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1260419","DOI":"10.1126\/science.1260419","article-title":"Proteomics. Tissue-based map of the human proteome","volume":"347","author":"Uhlen","year":"2015","journal-title":"Science"},{"key":"ref_62","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":"ref_63","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1093\/nar\/gks1224","article-title":"Implication of the SMN complex in the biogenesis and steady state level of the signal recognition particle","volume":"41","author":"Piazzon","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"8335","DOI":"10.1093\/nar\/gkw702","article-title":"The RNA-binding protein Gemin5 binds directly to the ribosome and regulates global translation","volume":"44","author":"Ramajo","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1016\/j.cell.2017.05.022","article-title":"The Mammalian Ribo-interactome Reveals Ribosome Functional Diversity and Heterogeneity","volume":"169","author":"Simsek","year":"2017","journal-title":"Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1093\/nar\/gkn979","article-title":"A novel role for Gemin5 in mRNA translation","volume":"37","author":"Pacheco","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"15662","DOI":"10.1074\/jbc.M115.646257","article-title":"Gemin5 Binds to the Survival Motor Neuron mRNA to Regulate SMN Expression","volume":"290","author":"Workman","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"7339","DOI":"10.1093\/nar\/gky361","article-title":"The landscape of the non-canonical RNA-binding site of Gemin5 unveils a feedback loop counteracting the negative effect on translation","volume":"46","author":"Dotu","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.bbagrm.2018.01.010","article-title":"Identification of the TXNIP IRES and characterization of the impact of regulatory IRES trans-acting factors","volume":"1861","author":"Lampe","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"8474","DOI":"10.1093\/nar\/gkx500","article-title":"An in vivo genetic screen for genes involved in spliced leader trans-splicing indicates a crucial role for continuous de novo spliced leader RNP assembly","volume":"45","author":"Philippe","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/s41536-020-0089-0","article-title":"A subset of SMN complex members have a specific role in tissue regeneration via ERBB pathway-mediated proliferation","volume":"5","author":"Pei","year":"2020","journal-title":"NPJ Regen. Med."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"4942","DOI":"10.1093\/nar\/gks172","article-title":"Gemin5 proteolysis reveals a novel motif to identify L protease targets","volume":"40","author":"Pineiro","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"5742","DOI":"10.1093\/nar\/gku177","article-title":"Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation","volume":"42","author":"Pineiro","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1093\/nar\/gkz1126","article-title":"Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control","volume":"48","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1101\/gad.291377.116","article-title":"Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5","volume":"30","author":"Jin","year":"2016","journal-title":"Genes Dev."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2376","DOI":"10.1101\/gad.288340.116","article-title":"Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly","volume":"30","author":"Xu","year":"2016","journal-title":"Genes Dev."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1038\/cr.2016.133","article-title":"Structural basis for specific recognition of pre-snRNA by Gemin5","volume":"26","author":"Tang","year":"2016","journal-title":"Cell Res."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1101\/gad.227843.113","article-title":"The role of disordered protein regions in the assembly of decapping complexes and RNP granules","volume":"27","author":"Jonas","year":"2013","journal-title":"Genes Dev."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/j.tibs.2003.10.007","article-title":"TPR proteins: The versatile helix","volume":"28","author":"Regan","year":"2003","journal-title":"Trends Biochem. Sci"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"e16761","DOI":"10.7554\/eLife.16761","article-title":"Origin of a folded repeat protein from an intrinsically disordered ancestor","volume":"5","author":"Zhu","year":"2016","journal-title":"Elife"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"e1800241","DOI":"10.1002\/bies.201800241","article-title":"Impact of RNA-Protein Interaction Modes on Translation Control: The Versatile Multidomain Protein Gemin5","volume":"41","author":"Azman","year":"2019","journal-title":"Bioessays"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"10697","DOI":"10.1073\/pnas.1502597112","article-title":"Dimerization of elongator protein 1 is essential for Elongator complex assembly","volume":"112","author":"Xu","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1021\/pr0504539","article-title":"Quantitative proteomics identifies Gemin5, a scaffolding protein involved in ribonucleoprotein assembly, as a novel partner for eukaryotic initiation factor 4E","volume":"5","author":"Mohammed","year":"2006","journal-title":"J. Proteome Res."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Bradrick, S.S., and Gromeier, M. (2009). Identification of Gemin5 as a novel 7-methylguanosine cap-binding protein. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0007030"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1038\/nature14427","article-title":"Structure of the human 80S ribosome","volume":"520","author":"Khatter","year":"2015","journal-title":"Nature"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/j.molcel.2007.02.015","article-title":"Ribosomal protein L3: Gatekeeper to the A site","volume":"25","author":"Meskauskas","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"3570","DOI":"10.1016\/j.jmb.2016.02.013","article-title":"Crystal Structures of the uL3 Mutant Ribosome: Illustration of the Importance of Ribosomal Proteins for Translation Efficiency","volume":"428","author":"Mailliot","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1016\/j.molcel.2015.03.029","article-title":"Coordinated Ribosomal L4 Protein Assembly into the Pre-Ribosome Is Regulated by Its Eukaryote-Specific Extension","volume":"58","author":"Stelter","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.cell.2016.01.003","article-title":"Redefining the Translational Status of 80S Monosomes","volume":"164","author":"Heyer","year":"2016","journal-title":"Cell"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"528","DOI":"10.3390\/biom5020528","article-title":"Gemin5: A Multitasking RNA-Binding Protein Involved in Translation Control","volume":"5","author":"Pineiro","year":"2015","journal-title":"Biomolecules"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1093\/nar\/gks1212","article-title":"Gemin5 promotes IRES interaction and translation control through its C-terminal region","volume":"41","author":"Pineiro","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4782","DOI":"10.1002\/pmic.200800338","article-title":"Riboproteomic analysis of polypeptides interacting with the internal ribosome-entry site element of foot-and-mouth disease viral RNA","volume":"8","author":"Pacheco","year":"2008","journal-title":"Proteomics"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.tim.2008.01.013","article-title":"The impact of RNA structure on picornavirus IRES activity","volume":"16","year":"2008","journal-title":"Trends Microbiol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/S0168-9525(00)02106-5","article-title":"Internal ribosome initiation of translation and the control of cell death","volume":"16","author":"Holcik","year":"2000","journal-title":"Trends Genet."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.cell.2009.01.042","article-title":"Regulation of translation initiation in eukaryotes: Mechanisms and biological targets","volume":"136","author":"Sonenberg","year":"2009","journal-title":"Cell"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1038\/nrm.2017.103","article-title":"Functional 5\u2032 UTR mRNA structures in eukaryotic translation regulation and how to find them","volume":"19","author":"Leppek","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"229","DOI":"10.4161\/cc.10.2.14472","article-title":"Cellular IRES-mediated translation: The war of ITAFs in pathophysiological states","volume":"10","author":"Komar","year":"2011","journal-title":"Cell Cycle"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/j.bbagrm.2014.09.012","article-title":"The role of IRES trans-acting factors in carcinogenesis","volume":"1849","author":"Faye","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Fernandez-Chamorro, J., Francisco-Velilla, R., Ramajo, J., and Martinez-Salas, E. (2019). Rab1b and ARF5 are novel RNA-binding proteins involved in FMDV IRES-driven RNA localization. Life Sci. Alliance, 2.","DOI":"10.26508\/lsa.201800131"},{"key":"ref_100","first-page":"2629","article-title":"Insights into Structural and Mechanistic Features of Viral IRES Elements","volume":"8","author":"Embarek","year":"2017","journal-title":"Front Microbiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.molcel.2019.01.017","article-title":"System-wide Profiling of RNA-Binding Proteins Uncovers Key Regulators of Virus Infection","volume":"74","author":"Noerenberg","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"9484","DOI":"10.1128\/JVI.01114-12","article-title":"Adaptive changes in alphavirus mRNA translation allowed colonization of vertebrate hosts","volume":"86","author":"Ventoso","year":"2012","journal-title":"J. Virol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/11\/3868\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:33:48Z","timestamp":1760175228000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/21\/11\/3868"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,5,29]]},"references-count":102,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2020,6]]}},"alternative-id":["ijms21113868"],"URL":"https:\/\/doi.org\/10.3390\/ijms21113868","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,5,29]]}}}