Sloan, Katherine E.

[["dc.bibliographiccitation.firstpage","237"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","247"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Watkins, Nicholas J."],["dc.date.accessioned","2018-11-07T09:19:15Z"],["dc.date.available","2018-11-07T09:19:15Z"],["dc.date.issued","2013"],["dc.description.abstract","Several proto-oncogenes and tumor suppressors regulate the production of ribosomes. Ribosome biogenesis is a major consumer of cellular energy, and defects result in p53 activation via repression of mouse double minute 2 (MDM2) homolog by the ribosomal proteins RPL5 and RPL11. Here, we report that RPL5 and RPL11 regulate p53 from the context of a ribosomal subcomplex, the 5S ribonucleoprotein particle (RNP). We provide evidence that the third component of this complex, the 5S rRNA, is critical for p53 regulation. In addition, we show that the 5S RNP is essential for the activation of p53 by p14(ARF), a protein that is activated by oncogene overexpression. Our data show that the abundance of the 5S RNP, and therefore p53 levels, is determined by factors regulating 5S complex formation and ribosome integration, including the tumor suppressor PICT1. The 5S RNP therefore emerges as the critical coordinator of signaling pathways that couple cell proliferation with ribosome production."],["dc.identifier.doi","10.1016/j.celrep.2013.08.049"],["dc.identifier.isi","000326152100024"],["dc.identifier.pmid","24120868"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10667"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28592"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","The 5S RNP Couples p53 Homeostasis to Ribosome Biogenesis and Nucleolar Stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4796"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","4809"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:23:54Z"],["dc.date.available","2018-11-07T10:23:54Z"],["dc.date.issued","2017"],["dc.description.abstract","Two proteins with PIN endonuclease domains, yUtp24(Fcf1)/hUTP24 and yUtp23/hUTP23 are essential for early pre-ribosomal (r) RNA cleavages at sites A0, A1/1 and A2/2a in yeast and humans. The yUtp24/hUTP24 PIN endonuclease is proposed to cleave at sites A1/1 and A2/2a, but the enzyme cleaving at site A0 is not known. Yeast yUtp23 contains a degenerate, non-essential PIN domain and functions together with the snR30 snoRNA, while human hUTP23 is associated with U17, the human snR30 counterpart. Using in vivo RNA-protein crosslinking and gel shift experiments, we reveal that yUtp23/hUTP23 makes direct contacts with expansion sequence 6 (ES6) in the 18S rRNA sequence and that yUtp23 interacts with the 3' half of the snR30 snoRNA. Protein-protein interaction studies further demonstrated that yeast yUtp23 and human hUTP23 directly interact with the H/ACA snoRNP protein yNhp2/hNHP2, the RNA helicase yRok1/hROK1(DDX52), the ribosome biogenesis factor yRrp7/hRRP7 and yUtp24/hUTP24. yUtp23/hUTP23 could therefore be central to the coordinated integration and release of ES6 binding factors and likely plays a pivotal role in remodeling this pre-rRNA region in both yeast and humans. Finally, studies using RNAi-rescue systems in human cells revealed that intact PIN domain and Zinc finger motifs in human hUTP23 are essential for 18S rRNA maturation."],["dc.identifier.doi","10.1093/nar/gkw1344"],["dc.identifier.isi","000400578600049"],["dc.identifier.pmid","28082392"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14964"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42551"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The ribosome biogenesis factor yUtp23/hUTP23 coordinates key interactions in the yeast and human pre-40S particle and hUTP23 contains an essential PIN domain"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Kudla, Grzegorz"],["dc.contributor.author","Tollervey, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:07:02Z"],["dc.date.available","2018-11-07T10:07:02Z"],["dc.date.issued","2016"],["dc.format.extent","9016"],["dc.identifier.doi","10.1093/nar/gkw645"],["dc.identifier.isi","000386945000043"],["dc.identifier.pmid","27418679"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39207"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans (vol 44, pg 5399, 2016)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","553"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","564"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Leisegang, Matthias S."],["dc.contributor.author","Doebele, Carmen"],["dc.contributor.author","Ramirez, Ana S."],["dc.contributor.author","Simm, Stefan"],["dc.contributor.author","Safferthal, Charlotta"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Schorge, Tobias"],["dc.contributor.author","Markoutsa, Stavroula"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Karas, Michael"],["dc.contributor.author","Ebersberger, Ingo"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T10:03:32Z"],["dc.date.available","2018-11-07T10:03:32Z"],["dc.date.issued","2015"],["dc.description.abstract","Translation fidelity and efficiency require multiple ribosomal (r)RNA modifications that are mostly mediated by small nucleolar (sno)RNPs during ribosome production. Overlapping basepairing of snoRNAs with pre-rRNAs often necessitates sequential and efficient association and dissociation of the snoRNPs, however, how such hierarchy is established has remained unknown so far. Here, we identify several late-acting snoRNAs that bind pre-40S particles in human cells and show that their association and function in pre-40S complexes is regulated by the RNA helicase DDX21. We map DDX21 crosslinking sites on pre-rRNAs and show their overlap with the basepairing sites of the affected snoRNAs. While DDX21 activity is required for recruitment of the late-acting snoRNAs SNORD56 and SNORD68, earlier snoRNAs are not affected by DDX21 depletion. Together, these observations provide an understanding of the timing and ordered hierarchy of snoRNP action in pre-40S maturation and reveal a novel mode of regulation of snoRNP function by an RNA helicase in human cells."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1093/nar/gku1291"],["dc.identifier.isi","000350207100052"],["dc.identifier.pmid","25477391"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11460"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38490"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","540"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","RNA-A PUBLICATION OF THE RNA SOCIETY"],["dc.bibliographiccitation.lastpage","550"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Schneider, Claudia"],["dc.contributor.author","Watkins, Nicholas J."],["dc.date.accessioned","2018-11-07T09:42:10Z"],["dc.date.available","2018-11-07T09:42:10Z"],["dc.date.issued","2014"],["dc.description.abstract","During eukaryotic ribosome biogenesis, three of the mature ribosomal (r)RNAs are released from a single precursor transcript (pre-rRNA) by an ordered series of endonucleolytic cleavages and exonucleolytic processing steps. Production of the 18S rRNA requires the removal of the 5 ' external transcribed spacer (5 ' ETS) by endonucleolytic cleavages at sites A0 and A1/site 1. In metazoans, an additional cleavage in the 5 ' ETS, at site A ', upstream of A0, has also been reported. Here, we have investigated how A ' processing is coordinated with assembly of the early preribosomal complex. We find that only the tUTP (UTP-A) complex is critical for A ' cleavage, while components of the bUTP (UTP-B) and U3 snoRNP are important, but not essential, for efficient processing at this site. All other factors involved in the early stages of 18S rRNA processing that were tested here function downstream from this processing step. Interestingly, we show that the RNA surveillance factors XRN2 and MTR4 are also involved in A ' cleavage in humans. A' cleavage is largely bypassed when XRN2 is depleted, and we also discover that A' cleavage is not always the initial processing event in all cell types. Together, our data suggest that A' cleavage is not a prerequisite for downstream pre-rRNA processing steps and may, in fact, represent a quality control step for initial pre-rRNA transcripts. Furthermore, we show that components of the RNA surveillance machinery, including the exosome and TRAMP complexes, also play key roles in the recycling of excised spacer fragments and degradation of aberrant pre-rRNAs in human cells."],["dc.identifier.doi","10.1261/rna.043471.113"],["dc.identifier.isi","000333191300011"],["dc.identifier.pmid","24550520"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33893"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1469-9001"],["dc.relation.issn","1355-8382"],["dc.title","The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5399"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5409"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Wells, Graeme R."],["dc.contributor.author","Weichmann, Franziska"],["dc.contributor.author","Colvin, David"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Kudla, Grzegorz"],["dc.contributor.author","Tollervey, David"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Schneider, Claudia"],["dc.date.accessioned","2018-11-07T10:12:41Z"],["dc.date.available","2018-11-07T10:12:41Z"],["dc.date.issued","2016"],["dc.description.abstract","During ribosomal RNA (rRNA) maturation, cleavages at defined sites separate the mature rRNAs from spacer regions, but the identities of several enzymes required for 18S rRNA release remain unknown. PilT N-terminus (PIN) domain proteins are frequently endonucleases and the PIN domain protein Utp24 is essential for early cleavages at three pre-rRNA sites in yeast (A0, A1 and A2) and humans (A0, 1 and 2a). In yeast, A1 is cleaved prior to A2 and both cleavages require base-pairing by the U3 snoRNA to the central pseudoknot elements of the 18S rRNA. We found that yeast Utp24 UV-crosslinked in vivo to U3 and the pseudoknot, placing Utp24 close to cleavage at site A1. Yeast and human Utp24 proteins exhibited in vitro endonuclease activity on an RNA substrate containing yeast site A2. Moreover, an intact PIN domain in human UTP24 was required for accurate cleavages at sites 1 and 2a in vivo, whereas mutation of another potential site 2a endonuclease, RCL1, did not affect 18S production. We propose that Utp24 cleaves sites A1/1 and A2/2a in yeast and human cells."],["dc.identifier.doi","10.1093/nar/gkw213"],["dc.identifier.isi","000379753100044"],["dc.identifier.pmid","27034467"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40287"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]