Bohnsack, Markus T.

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Birikmen, Mehmet"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Tran, Vinh"],["dc.contributor.author","Somayaji, Sharvari"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Ebersberger, Ingo"],["dc.date.accessioned","2021-12-01T09:24:03Z"],["dc.date.available","2021-12-01T09:24:03Z"],["dc.date.issued","2021"],["dc.description.abstract","Ribosome assembly is an essential and carefully choreographed cellular process. In eukaryotes, several 100 proteins, distributed across the nucleolus, nucleus, and cytoplasm, co-ordinate the step-wise assembly of four ribosomal RNAs (rRNAs) and approximately 80 ribosomal proteins (RPs) into the mature ribosomal subunits. Due to the inherent complexity of the assembly process, functional studies identifying ribosome biogenesis factors and, more importantly, their precise functions and interplay are confined to a few and very well-established model organisms. Although best characterized in yeast ( Saccharomyces cerevisiae ), emerging links to disease and the discovery of additional layers of regulation have recently encouraged deeper analysis of the pathway in human cells. In archaea, ribosome biogenesis is less well-understood. However, their simpler sub-cellular structure should allow a less elaborated assembly procedure, potentially providing insights into the functional essentials of ribosome biogenesis that evolved long before the diversification of archaea and eukaryotes. Here, we use a comprehensive phylogenetic profiling setup, integrating targeted ortholog searches with automated scoring of protein domain architecture similarities and an assessment of when search sensitivity becomes limiting, to trace 301 curated eukaryotic ribosome biogenesis factors across 982 taxa spanning the tree of life and including 727 archaea. We show that both factor loss and lineage-specific modifications of factor function modulate ribosome biogenesis, and we highlight that limited sensitivity of the ortholog search can confound evolutionary conclusions. Projecting into the archaeal domain, we find that only few factors are consistently present across the analyzed taxa, and lineage-specific loss is common. While members of the Asgard group are not special with respect to their inventory of ribosome biogenesis factors (RBFs), they unite the highest number of orthologs to eukaryotic RBFs in one taxon. Using large ribosomal subunit maturation as an example, we demonstrate that archaea pursue a simplified version of the corresponding steps in eukaryotes. Much of the complexity of this process evolved on the eukaryotic lineage by the duplication of ribosomal proteins and their subsequent functional diversification into ribosome biogenesis factors. This highlights that studying ribosome biogenesis in archaea provides fundamental information also for understanding the process in eukaryotes."],["dc.description.abstract","Ribosome assembly is an essential and carefully choreographed cellular process. In eukaryotes, several 100 proteins, distributed across the nucleolus, nucleus, and cytoplasm, co-ordinate the step-wise assembly of four ribosomal RNAs (rRNAs) and approximately 80 ribosomal proteins (RPs) into the mature ribosomal subunits. Due to the inherent complexity of the assembly process, functional studies identifying ribosome biogenesis factors and, more importantly, their precise functions and interplay are confined to a few and very well-established model organisms. Although best characterized in yeast ( Saccharomyces cerevisiae ), emerging links to disease and the discovery of additional layers of regulation have recently encouraged deeper analysis of the pathway in human cells. In archaea, ribosome biogenesis is less well-understood. However, their simpler sub-cellular structure should allow a less elaborated assembly procedure, potentially providing insights into the functional essentials of ribosome biogenesis that evolved long before the diversification of archaea and eukaryotes. Here, we use a comprehensive phylogenetic profiling setup, integrating targeted ortholog searches with automated scoring of protein domain architecture similarities and an assessment of when search sensitivity becomes limiting, to trace 301 curated eukaryotic ribosome biogenesis factors across 982 taxa spanning the tree of life and including 727 archaea. We show that both factor loss and lineage-specific modifications of factor function modulate ribosome biogenesis, and we highlight that limited sensitivity of the ortholog search can confound evolutionary conclusions. Projecting into the archaeal domain, we find that only few factors are consistently present across the analyzed taxa, and lineage-specific loss is common. While members of the Asgard group are not special with respect to their inventory of ribosome biogenesis factors (RBFs), they unite the highest number of orthologs to eukaryotic RBFs in one taxon. Using large ribosomal subunit maturation as an example, we demonstrate that archaea pursue a simplified version of the corresponding steps in eukaryotes. Much of the complexity of this process evolved on the eukaryotic lineage by the duplication of ribosomal proteins and their subsequent functional diversification into ribosome biogenesis factors. This highlights that studying ribosome biogenesis in archaea provides fundamental information also for understanding the process in eukaryotes."],["dc.identifier.doi","10.3389/fmicb.2021.739000"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94834"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-302X"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Tracing Eukaryotic Ribosome Biogenesis Factors Into the Archaeal Domain Sheds Light on the Evolution of Functional Complexity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Trends in Biochemical Sciences"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Kleiber, Nicole"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2022-04-06T07:33:28Z"],["dc.date.available","2022-04-06T07:33:28Z"],["dc.date.issued","2022-03-29"],["dc.description.abstract","Modified nucleotides within cellular RNAs significantly influence their biogenesis, stability, and function. As reviewed here, 3-methylcytidine (m3C) has recently come to the fore through the identification of the methyltransferases responsible for installing m3C32 in human tRNAs. Mechanistic details of how m3C32 methyltransferases recognize their substrate tRNAs have been uncovered and the biogenetic and functional relevance of interconnections between m3C32 and modified adenosines at position 37 highlighted. Functional insights into the role of m3C32 modifications indicate that they influence tRNA structure and, consistently, lack of m3C32 modifications impairs translation. Development of quantitative, transcriptome-wide m3C mapping approaches and the discovery of an m3C demethylase reveal m3C to be dynamic, raising the possibility that it contributes to fine-tuning gene expression in different conditions."],["dc.identifier.doi","10.1016/j.tibs.2022.03.004"],["dc.identifier.pmid","35365384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106432"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/468"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/174"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.issn","0968-0004"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Roles and dynamics of 3-methylcytidine in cellular RNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1009407"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Pätz, Christina"],["dc.contributor.author","Akkermann, Dagmar"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Galka, Dajana"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-04-14T08:28:05Z"],["dc.date.available","2021-04-14T08:28:05Z"],["dc.date.issued","2021"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1371/journal.pgen.1009407"],["dc.identifier.pmid","33657088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82500"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/140"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","1553-7404"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY 4.0"],["dc.title","DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","6152"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Krogh, Nicolai"],["dc.contributor.author","Pan, Kuan-Ting"],["dc.contributor.author","Jaafar, Mariam"],["dc.contributor.author","Henras, Anthony K."],["dc.contributor.author","Nielsen, Henrik"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-12-01T09:20:51Z"],["dc.date.available","2021-12-01T09:20:51Z"],["dc.date.issued","2021"],["dc.description.abstract","Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41467-021-26208-9"],["dc.identifier.pii","26208"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94285"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.title","The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8074"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","8089"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Ferreira, Rafael Rinaldi"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Gruber, Jens"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-04-14T08:24:14Z"],["dc.date.available","2021-04-14T08:24:14Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1093/nar/gkaa549"],["dc.identifier.pmid","32609813"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17489"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81210"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/53"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/116"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The human box C/D snoRNA U3 is a miRNA source and miR-U3 regulates expression of sortin nexin 27"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","209"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Kleiber, Nicole"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Stiller, Carina"],["dc.contributor.author","Heinrichs, Marleen"],["dc.contributor.author","Mai, Mandy Mong-Quyen"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2022-02-01T10:31:09Z"],["dc.date.available","2022-02-01T10:31:09Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Modified nucleotides in tRNAs are important determinants of folding, structure and function. Here we identify METTL8 as a mitochondrial matrix protein and active RNA methyltransferase responsible for installing m 3 C 32 in the human mitochondrial (mt-)tRNA Thr and mt-tRNA Ser(UCN) . METTL8 crosslinks to the anticodon stem loop (ASL) of many mt-tRNAs in cells, raising the question of how methylation target specificity is achieved. Dissection of mt-tRNA recognition elements revealed U 34 G 35 and t 6 A 37 /(ms 2 )i 6 A 37 , present concomitantly only in the ASLs of the two substrate mt-tRNAs, as key determinants for METTL8-mediated methylation of C 32 . Several lines of evidence demonstrate the influence of U 34 , G 35 , and the m 3 C 32 and t 6 A 37 /(ms 2 )i 6 A 37 modifications in mt-tRNA Thr/Ser(UCN) on the structure of these mt-tRNAs. Although mt-tRNA Thr/Ser(UCN) lacking METTL8-mediated m 3 C 32 are efficiently aminoacylated and associate with mitochondrial ribosomes, mitochondrial translation is mildly impaired by lack of METTL8. Together these results define the cellular targets of METTL8 and shed new light on the role of m 3 C 32 within mt-tRNAs."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.1038/s41467-021-27905-1"],["dc.identifier.pii","27905"],["dc.identifier.pmid","35017528"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98794"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/390"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/167"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The RNA methyltransferase METTL8 installs m3C32 in mitochondrial tRNAsThr/Ser(UCN) to optimise tRNA structure and mitochondrial translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","54"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Journal of Heart Failure"],["dc.bibliographiccitation.lastpage","66"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Berulava, Tea"],["dc.contributor.author","Buchholz, Eric"],["dc.contributor.author","Elerdashvili, Vakhtang"],["dc.contributor.author","Pena, Tonatiuh"],["dc.contributor.author","Islam, Md Rezaul"],["dc.contributor.author","Lbik, Dawid"],["dc.contributor.author","Mohamed, Belal A."],["dc.contributor.author","Renner, Andre"],["dc.contributor.author","Lewinski, Dirk"],["dc.contributor.author","Sacherer, Michael"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Jain, Gaurav"],["dc.contributor.author","Capece, Vincenzo"],["dc.contributor.author","Cleve, Nicole"],["dc.contributor.author","Burkhardt, Susanne"],["dc.contributor.author","Hasenfuss, Gerd"],["dc.contributor.author","Fischer, Andre"],["dc.contributor.author","Toischer, Karl"],["dc.date.accessioned","2020-12-10T14:06:19Z"],["dc.date.available","2020-12-10T14:06:19Z"],["dc.date.issued","2019"],["dc.description.abstract","ABSTRACT Aims Deregulation of epigenetic processes and aberrant gene expression are important mechanisms in heart failure. Here we studied the potential relevance of m6A RNA methylation in heart failure development. Methods and results We analysed m6A RNA methylation via next‐generation sequencing. We found that approximately one quarter of the transcripts in the healthy mouse and human heart exhibit m6A RNA methylation. During progression to heart failure we observed that changes in m6A RNA methylation exceed changes in gene expression both in mouse and human. RNAs with altered m6A RNA methylation were mainly linked to metabolic and regulatory pathways, while changes in RNA expression level mainly represented changes in structural plasticity. Mechanistically, we could link m6A RNA methylation to altered RNA translation and protein production. Interestingly, differentially methylated but not differentially expressed RNAs showed differential polysomal occupancy, indicating transcription‐independent modulation of translation. Furthermore, mice with a cardiomyocyte restricted knockout of the RNA demethylase Fto exhibited an impaired cardiac function compared to control mice. Conclusions We could show that m6A landscape is altered in heart hypertrophy and heart failure. m6A RNA methylation changes lead to changes in protein abundance, unconnected to mRNA levels. This uncovers a new transcription‐independent mechanisms of translation regulation. Therefore, our data suggest that modulation of epitranscriptomic processes such as m6A methylation might be an interesting target for therapeutic interventions."],["dc.description.sponsorship","German Center for cardiovascular research (DZHK)"],["dc.description.sponsorship","German Center for Neurodegenerative Diseases (DZNE) http://dx.doi.org/10.13039/501100005224"],["dc.description.sponsorship","BMBF http://dx.doi.org/10.13039/501100002347"],["dc.description.sponsorship","German Research Foundation (DFG"],["dc.identifier.doi","10.1002/ejhf.1672"],["dc.identifier.pmid","31849158"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17076"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69851"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/11"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/334"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | D01: Erholung aus der Herzinsuffizienz – Einfluss von Fibrose und Transkriptionssignatur"],["dc.relation","SFB 1002 | D04: Bedeutung der Methylierung von RNA (m6A) und des Histons H3 (H3K4) in der Herzinsuffizienz"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG A. Fischer (Epigenetics and Systems Medicine in Neurodegenerative Diseases)"],["dc.relation.workinggroup","RG Hasenfuß"],["dc.relation.workinggroup","RG Toischer (Kardiales Remodeling)"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","Changes in m6A RNA methylation contribute to heart failure progression by modulating translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["cris.virtual.author-orcid","0000-0001-6035-4255"],["cris.virtual.author-orcid","0000-0001-7063-5456"],["cris.virtual.department","Universitätsmedizin Göttingen"],["cris.virtual.department","Universitätsmedizin Göttingen"],["cris.virtualsource.author-orcid","47ac62af-19cd-4011-895b-a6ab85d91e81"],["cris.virtualsource.author-orcid","145b86b4-d1b9-4744-8517-cdde207804bc"],["cris.virtualsource.department","47ac62af-19cd-4011-895b-a6ab85d91e81"],["cris.virtualsource.department","145b86b4-d1b9-4744-8517-cdde207804bc"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T18:42:37Z"],["dc.date.available","2020-12-10T18:42:37Z"],["dc.date.issued","2019"],["dc.description.abstract","The essential cellular process of ribosome biogenesis is at the nexus of various signalling pathways that coordinate protein synthesis with cellular growth and proliferation. The fact that numerous diseases are caused by defects in ribosome assembly underscores the importance of obtaining a detailed understanding of this pathway. Studies in yeast have provided a wealth of information about the fundamental principles of ribosome assembly, and although many features are conserved throughout eukaryotes, the larger size of human (pre-)ribosomes, as well as the evolution of additional regulatory networks that can modulate ribosome assembly and function, have resulted in a more complex assembly pathway in humans. Notably, many ribosome biogenesis factors conserved from yeast appear to have subtly different or additional functions in humans. In addition, recent genome-wide, RNAi-based screens have identified a plethora of novel factors required for human ribosome biogenesis. In this review, we discuss key aspects of human ribosome production, highlighting differences to yeast, links to disease, as well as emerging concepts such as extra-ribosomal functions of ribosomal proteins and ribosome heterogeneity."],["dc.identifier.doi","10.15252/embj.2018100278"],["dc.identifier.pmid","31088842"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78024"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/70"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Uncovering the assembly pathway of human ribosomes and its emerging links to disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]