The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs
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The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.
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Catalytic activities of the RNA exosome are mediated by associated 3'−5' exonucleases EXOSC10 and DIS3 or accessory factors such as MTR4, while core components including EXOSC3 provide structural stability and facilitate substrate recognition and/or RNA threading.
“The catalytic activities of the RNA exosome are mediated by associated 3’−5’ exonucleases EXOSC10 and DIS3 or accessory factors such as the RNA helicase MTR4, while core components including EXOSC3 provide structural stability and facilitate substrate recognition and/or RNA threading through the protein complex core39–43.”
From EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery (2026) · cites this paper as [40]
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Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
<i>Phaser</i> crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
Piotto, M., Saudek, V., & Sklenář, V. (1992) · Journal of Biomolecular NMR · doi:10.1007/bf02192855 · Cited by 3,720 · see citing works
The CCPN data model for NMR spectroscopy: Development of a software pipeline
Vranken, W., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinás, M., Ulrich, E. L., Markley, J. L., Ionides, J., & Laue, E. D. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20449 · Cited by 3,222 · see citing works
Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T. J., Forman-Kay, J. D., & Kay, L. E. (1994) · Biochemistry · doi:10.1021/bi00185a040 · Cited by 2,094 · see citing works
Sattler, M. (1999) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(98)00025-9 · Cited by 1,770 · see citing works
Self-citationxia2 : an expert system for macromolecular crystallography data reduction
Winter, G. (2009) · Journal of Applied Crystallography · doi:10.1107/s0021889809045701 · Cited by 1,530 · see citing works
Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
Painter, J., & Merritt, E. A. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906005270 · Cited by 1,244 · see citing works
Tommaso, P. D., Moretti, S., Xénarios, I., Orobitg, M., Montanyola, A., Chang, J., Taly, J.-F., & Notredame, C. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr245 · Cited by 1,170 · see citing works
DIALS : implementation and evaluation of a new integration package
Winter, G., Waterman, D. G., Parkhurst, J. M., Brewster, A. S., Gildea, R. J., Gerstel, M., Fuentes‐Montero, L., Vollmar, M., Michels-Clark, T., Young, I. D., et al. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317017235 · Cited by 1,128 · see citing works
Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M., & Tollervey, D. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80432-8 · Cited by 947 · see citing works
Grzesiek, S., & Bax, A. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00079a052 · Cited by 892 · see citing works
RNA Degradation by the Exosome Is Promoted by a Nuclear Polyadenylation Complex
LaCava, J., Houseley, J. M., Saveanu, C., Petfalski, E., Thompson, E., Jacquier, A., & Tollervey, D. W. (2005) · Cell · doi:10.1016/j.cell.2005.04.029 · Cited by 870 · see citing works
Wyers, F., Rougemaille, M., Badis, G., Rousselle, J.-C., Dufour, M., Boulay, J., Regnault, B., Devaux, F., Namane, A., Séraphin, B., et al. (2005) · Cell · doi:10.1016/j.cell.2005.04.030 · Cited by 843 · see citing works
Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
Meyer, H. H., Bug, M., & Bremer, S. (2012) · Nature Cell Biology · doi:10.1038/ncb2407 · Cited by 803 · see citing works
BAC TransgeneOmics: a high-throughput method for exploration of protein function in mammals
Poser, I., Sarov, M., Hutchins, J. R. A., Hèriché, J.-K., Toyoda, Y., Pozniakovsky, A., Weigl, D., Nitzsche, A., Hegemann, B., Bird, A. W., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1199 · Cited by 597 · see citing works
A New Yeast Poly(A) Polymerase Complex Involved in RNA Quality Control
Vaňáčová, Š., Wolf, J., Martin, G., Blank, D., Dettwiler, S., Friedlein, A., Langen, H., Keith, G., & Keller, W. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030189 · Cited by 567 · see citing works
Reconstitution, Activities, and Structure of the Eukaryotic RNA Exosome
Liu, Q., Greimann, J. C., & Lima, C. D. (2006) · Cell · doi:10.1016/j.cell.2006.10.037 · Cited by 544 · see citing works
CCP 4 i 2: the new graphical user interface to the CCP 4 program suite
Potterton, L., Agirre, J., Ballard, C. B., Cowtan, K. D., Dodson, E. J., Evans, P. R., Jenkins, H. T., Keegan, R. M., Krissinel, E., Stevenson, K., et al. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317016035 · Cited by 535 · see citing works
The regulation and functions of the nuclear RNA exosome complex
Kilchert, C., Wittmann, S., & Vasiljeva, L. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2015.15 · Cited by 444 · see citing works
Interaction Profiling Identifies the Human Nuclear Exosome Targeting Complex
Lubas, M., Christensen, M. S., Kristiansen, M. S., Domanski, M., Falkenby, L. G., Lykke‐Andersen, S., Andersen, J., Dziembowski, A., & Jensen, T. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.028 · Cited by 422 · see citing works
A single subunit, Dis3, is essentially responsible for yeast exosome core activity
Dziembowski, A., Lorentzen, E., Conti, E., & Séraphin, B. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1184 · Cited by 421 · see citing works
Self-citationIdentification of a Nuclear Exosome Decay Pathway for Processed Transcripts
Meola, N., Domanski, M., Karadoulama, E., Chen, Y., Gentil, C., Pultz, D., Vitting-Seerup, K., Lykke-Andersen, S., Andersen, J. S., Sandelin, A., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.025 · Cited by 290 · see citing works
Tudor Domains Bind Symmetrical Dimethylated Arginines
Côté, J., & Richard, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414328200 · Cited by 261 · see citing works
RNA decay machines: The exosome
Chlebowski, A., Lubas, M., Jensen, T. H., & Dziembowski, A. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.01.006 · Cited by 246 · see citing works
Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactorsPreprint
Zinder, J. C., & Lima, C. D. (2017) · Genes & Development · doi:10.1101/gad.294769.116 · Cited by 234 · see citing works
Control of p97 function by cofactor binding
Buchberger, A., Schindelin, H., & Hänzelmann, P. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.08.028 · Cited by 219 · see citing works
Kadaba, S., Wang, X., & Anderson, J. T. (2006) · RNA · doi:10.1261/rna.2305406 · Cited by 208 · see citing works
Lubas, M., Andersen, P. R., Schein, A., Dziembowski, A., Kudla, G., & Jensen, T. H. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.026 · Cited by 201 · see citing works
The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins
Thoms, M., Thomson, E., Baßler, J., Gnädig, M., Griesel, S., & Hurt, E. (2015) · Cell · doi:10.1016/j.cell.2015.07.060 · Cited by 192 · see citing works
Weick, E.-M., Puno, M. R., Januszyk, K., Zinder, J. C., DiMattia, M. A., & Lima, C. D. (2018) · Cell · doi:10.1016/j.cell.2018.05.041 · Cited by 153 · see citing works
Weir, J. R., Bonneau, F., Hentschel, J., & Conti, E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004953107 · Cited by 147 · see citing works
Self-citationOgami, K., Richard, P., Chen, Y., Hoque, M., Li, W., Moresco, J. J., Yates, J. R., Tian, B., & Manley, J. L. (2017) · Genes & Development · doi:10.1101/gad.302604.117 · Cited by 143 · see citing works
Structure of the nuclear exosome captured on a maturing preribosome
Schuller, J. M., Falk, S., Fromm, L., Hurt, E., & Conti, E. (2018) · Science · doi:10.1126/science.aar5428 · Cited by 124 · see citing works
Self-citationThe crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing
Jackson, R. N., Klauer, A. A., Hintze, B. J., Robinson, H., van Hoof, A., & Johnson, S. J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.107 · Cited by 121 · see citing works
The exosome‐binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase
Schuch, B., Feigenbutz, M., Makino, D. L., Falk, S., Minard‐Basquin, C., Mitchell, P., & Conti, E. (2014) · The EMBO Journal · doi:10.15252/embj.201488757 · Cited by 110 · see citing works
Self-citationMPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation
Schilders, G. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki982 · Cited by 109 · see citing works
Silla, T., Karadoulama, E., Mąkosa, D., Lubas, M., & Jensen, T. H. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.061 · Cited by 95 · see citing works
Milligan, L., Decourty, L., Saveanu, C., Rappsilber, J., Ceulemans, H., Jacquier, A., & Tollervey, D. W. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00463-08 · Cited by 94 · see citing works
Ski2-like RNA helicase structures
Johnson, S. J., & Jackson, R. N. (2012) · RNA Biology · doi:10.4161/rna.22101 · Cited by 93 · see citing works
The RNA exosome and proteasome: common principles of degradation control
Makino, D. L., Halbach, F., & Conti, E. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3657 · Cited by 82 · see citing works
Self-citationHänzelmann, P., & Schindelin, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.274506 · Cited by 80 · see citing works
Falk, S., Weir, J. R., Hentschel, J., Reichelt, P., Bonneau, F., & Conti, E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.07.020 · Cited by 77 · see citing works
Self-citationRNA Surveillance by the Nuclear RNA Exosome: Mechanisms and Significance
Ogami, K., Chen, Y., & Manley, J. L. (2018) · Non-Coding RNA · doi:10.3390/ncrna4010008 · Cited by 75 · see citing works
Rrp6, Rrp47 and Cofactors of the Nuclear Exosome
Butler, J. S., & Mitchell, P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7841-7_8 · Cited by 62 · see citing works
Puno, M. R., & Lima, C. D. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803530115 · Cited by 62 · see citing works
Distinct and evolutionary conserved structural features of the human nuclear exosome complex
Gerlach, P., Schuller, J. M., Bonneau, F., Basquin, J., Reichelt, P., Falk, S., & Conti, E. (2018) · eLife · doi:10.7554/elife.38686 · Cited by 59 · see citing works
Self-citationStructure of the RBM7–ZCCHC8 core of the NEXT complex reveals connections to splicing factors
Falk, S., Finogenova, K., Melko, M., Benda, C., Lykke‐Andersen, S., Jensen, T. H., & Conti, E. (2016) · Nature Communications · doi:10.1038/ncomms13573 · Cited by 52 · see citing works
Self-citationMpp6 Incorporation in the Nuclear Exosome Contributes to RNA Channeling through the Mtr4 Helicase
Falk, S., Bonneau, F., Ebert, J., Kögel, A., & Conti, E. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.033 · Cited by 52 · see citing works
Self-citationCarneiro, T., Carvalho, C., Braga, J., Rino, J., Milligan, L., Tollervey, D. W., & Carmo‐Fonseca, M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00120-07 · Cited by 52 · see citing works
NRDE2 negatively regulates exosome functions by inhibiting MTR4 recruitment and exosome interactionPreprint
Wang, J., Chen, J., Wu, G., Zhang, H., Du, X., Chen, S., Zhang, L., Wang, K., Fan, J., Gao, S., et al. (2019) · Genes & Development · doi:10.1101/gad.322602.118 · Cited by 47 · see citing works
Falk, S., Tants, J., Basquin, J., Thoms, M., Hurt, E., Sattler, M., & Conti, E. (2017) · RNA · doi:10.1261/rna.062901.117 · Cited by 42 · see citing works
Self-citationNagahama, M., Yamazoe, T., Hara, Y., Tani, K., Tsuji, A., & Tagaya, M. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.017 · Cited by 35 · see citing works
Hiraishi, N., Ishida, Y.-I., Sudo, H., & Nagahama, M. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.10.148 · Cited by 32 · see citing works
AAA-ATPase NVL2 acts on MTR4-exosome complex to dissociate the nucleolar protein WDR74
Hiraishi, N., Ishida, Y.-I., & Nagahama, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.09.160 · Cited by 26 · see citing works
Zcchc8 is a glycogen synthase kinase-3 substrate that interacts with RNA-binding proteins
Gustafson, M. P., Welcker, M., Hwang, H. C., & Clurman, B. E. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.10.090 · Cited by 24 · see citing works
Structure of an atypical Tudor domain in the Drosophila Polycomblike protein
Friberg, A., Oddone, A., Klymenko, T., Müller, J., & Sattler, M. (2010) · Protein Science · doi:10.1002/pro.476 · Cited by 21 · see citing works
Self-citationFujiwara, Y., Fujiwara, K., Goda, N., Iwaya, N., Tenno, T., Shirakawa, M., & Hiroaki, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174680 · Cited by 21 · see citing works
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Revy, P., Kannengiesser, C., & Bertuch, A. A. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00527-z · Cited by 243 · see citing works
ELM—the Eukaryotic Linear Motif resource—2024 update
Kumar, M., Michael, S., Alvarado-Valverde, J., Zeke, A., Lázár, T., Glavina, J., Nagy‐Kanta, E., Donagh, J. M., Kálmán, Z. E., Pascarelli, S., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1058 · Cited by 185 · see citing works
Cellular functions of eukaryotic RNA helicases and their links to human diseases
Bohnsack, K. E., Yi, S., Venus, S., Jankowsky, E., & Bohnsack, M. T. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00628-5 · Cited by 131 · see citing works
Garland, W., Müller, I. I., Wu, M., Schmid, M., Imamura, K., Rib, L., Sandelin, A., Helin, K., & Jensen, T. H. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.004 · Cited by 93 · see citing works
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Puno, M. R., & Lima, C. D. (2022) · Cell · doi:10.1016/j.cell.2022.04.016 · Cited by 55 · see citing works
Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.011 · Cited by 55 · see citing works
Self-citationWang, Y., Yu, Y., Pang, Y., Yu, H., Zhang, W., Zhao, X., & Yu, J. (2021) · RNA Biology · doi:10.1080/15476286.2021.1909320 · Cited by 55 · see citing works
Kögel, A., Keidel, A., Bonneau, F., Schäfer, I. B., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.01.009 · Cited by 51 · see citing works
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Ruiz, J. C., Devlin, A. M., Kim, J., & Conrad, N. K. (2020) · Journal of Virology · doi:10.1128/jvi.00287-20 · Cited by 9 · see citing works
Out or decay: fate determination of nuclear RNAs
Wang, J., & Cheng, H. (2020) · Essays in Biochemistry · doi:10.1042/ebc20200005 · Cited by 8 · see citing works
Monitoring Protein-RNA Interaction Dynamics in vivo at High Temporal Resolution using χCRAC
McKellar, S. W., Ivanova, I., van Nues, R. W., Cordiner, R. A., Chauhan, M., Christopoulou, N., Worboys, W., Langford, A., Jensen, T. H., & Granneman, S. (2020) · Journal of Visualized Experiments · doi:10.3791/61027 · Cited by 8 · see citing works
Tu, S., Zou, J., Xiong, C., Dai, C., Sun, H., Luo, D., Jin, M., Chen, H., & Zhou, H. (2024) · Journal of Virology · doi:10.1128/jvi.00796-24 · Cited by 7 · see citing works
A UTP3-dependent nucleolar translocation pathway facilitates pre-rRNA 5′ETS processing
Bao, J., Su, B., Chen, Z., Sun, Z., Peng, J., & Zhao, S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae631 · Cited by 7 · see citing works
Communication network within the essential AAA-ATPase Rix7 drives ribosome assembly
Kocaman, S., Lo, Y., Krahn, J. M., Sobhany, M., Dandey, V. P., Petrovich, M., Etigunta, S. K., Williams, J. G., Deterding, L. J., Borgnia, M. J., et al. (2022) · PNAS Nexus · doi:10.1093/pnasnexus/pgac118 · Cited by 5 · see citing works
Assembly of multicomponent machines in RNA metabolism: A common theme in mRNA decay pathways
de Amorim, A. M., & Chakrabarti, S. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1684 · Cited by 5 · see citing works
RNA-binding protein Mub1 and the nuclear RNA exosome act to fine-tune environmental stress response
Birot, A., Kilchert, C., Kuś, K., Priest, E., Alwash, A. A., Castelló, A., Mohammed, S., & Vasiljeva, L. (2021) · Life Science Alliance · doi:10.26508/lsa.202101111 · Cited by 5 · see citing works
MTR4 adaptor PICT1 functions in two distinct steps during pre-rRNA processing
Miyao, S., Saito, K., Oshima, R., Kawahara, K., & Nagahama, M. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.11.018 · Cited by 5 · see citing works
Majerčiak, V., Alvarado-Hernandez, B., Ma, Y., Duduskar, S. N., Lobanov, A. V., Cam, M., & Zheng, Z. (2024) · mBio · doi:10.1128/mbio.03172-24 · Cited by 4 · see citing works
Samajdar, A., Amato, R., Jo, S., Cordes, E., Tai, A., Raffa, G. D., & Batista, L. F. Z. (2026) · Genes & Development · doi:10.1101/gad.353100.125 · Cited by 3 · see citing works
Pan-cancer analysis portrays NVL2 as a novel diagnostic and prognostic biomarker
Datta, M., & Nayak, A. (2023) · Human Gene · doi:10.1016/j.humgen.2023.201254 · Cited by 2 · see citing works
TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2
Denson, J., Zhang, N., Ball, D., Thompson, K., Johnson, S., & D’Arcy, S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2414980121 · Cited by 2 · see citing works
Conserved Residues at the Mtr4 C-Terminus Coordinate Helicase Activity and Exosome Interactions
Yim, M., Stuart, C. J., Pond, M. I., van Hoof, A., & Johnson, S. J. (2023) · Biochemistry · doi:10.1021/acs.biochem.3c00401 · Cited by 2 · see citing works
EXOSC3 G191 Variants Trigger System-Wide Recalibration of RNA Processing Machinery
Wijeratne, H. R. S., Runnebohm, A. M., Barron, M. P., Hampton, A. J., Li, R., Peck Justice, S. A., Lenceski, S. H., Rooney, J. D., Smith-Kinnaman, W. R., Chang, G. S., et al. (2026) · doi:10.64898/2026.01.26.701775 · Cited by 1 · see citing works
Sadic, M., Schneider, W. M., Katsara, O., Medina, G. N., Mogulothu, A., Yu, Y., Gu, M., Santos, T. D. L., Schneider, R. J., & Dittmann, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.08.479557
McKellar, S. W., Ivanova, I., van Nues, R. W., Cordiner, R. A., Chauhan, M., Christopoulou, N., Worboys, W., Langford, A., Jensen, T. H., & Granneman, S. (2020) · doi:10.3791/61027-v
de Camargo, J. B. B., Bittencourt, D., Michel, J. M., da Silva, D. G., Bergamasco, J. G. A., Tiede, D., Lewis, D. T., Nacafucasaco, E. T. A., Ferrari, O., Melo, A. C. C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.23.707462
ORF57/MTA in KSHV biology and pathogenesis: update from 2015
Zheng, Z.-M., & Majerciak, V. (2026) · Journal of Medical Virology · doi:10.1002/jmv.70979
The RNA exosome: mechanisms of RNA surveillance, regulation, and disease
Upadhyai, P., Quadri, N., & Chandran, D. (2026) · RNA Biology · doi:10.1080/15476286.2026.2685379
Phosphorylation Patterns of Preribosomal Proteins Associated with the RNA Exosome
Almeida, F. A., Neto, V. G., Jantsch, R. B., Barros, M. R. A., Cepeda, L. P. P., Queiroz, B. R. S., Machado, A. B. E., Menezes, A. P. D. J., da Cunha, J. P., & Oliveira, C. C. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00095
de Camargo, J. B. B., Bittencourt, D., Michel, J. M., da Silva, D. G., Bergamasco, J. G. A., Berry, A. C., Tiede, D., Lewis, D., Nacafucasaco, E. T. A., Ferrari, O., et al. (2026) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00284.2026 · Cited by 2 · see citing works
Li, Y.-J., Tian, K.-Y., Li, S.-L., Wang, Y., Cao, Q., Wang, S.-H., Zhang, X.-H., Wang, X.-G., Lian, H.-G., Liu, X., et al. (2026) · Biochimica et Biophysica Acta - Molecular Basis of Disease · doi:10.1016/j.bbadis.2026.168374
DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly
Pisano, A., Bourdeaux, J., Mazur, J., Roses, F., Roméo, Y., Petfalski, E., Arx, T. V., Portugal-Calisto, D., Oborská‐Oplová, M., Peña, C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76536-x
The cellular landscape of druggable RNA-binding proteins
Timoteo, G. D., George, B. M., Abdel-Wahab, O. I., Flynn, R. A., & Tzelepis, K. (2026) · Nature Reviews Drug Discovery · doi:10.1038/s41573-026-01531-2
- Authors
- Lingaraju, M., Johnsen, D., Schlundt, A., Langer, L. M., Basquin, J., Sattler, M., Heick Jensen, T., Falk, S., & Conti, E.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- Aarhus University (DK)
- Goethe University Frankfurt (DE)
- Center for Integrated Protein Science Munich (DE)
- University of Vienna (AT)
- Corresponding author
- Falk, Sebastian
- Conti, Elena
- Venue
- Nature Communications
- Published
- 2019-07-29
- Volume
- 10
- Issue
- 1
- Pages
- 3393-3393
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6662825
- OpenAlex
- W2964712519
- Cited by
- 55
- References
- 60
- Citations by year
- 2026: 10 · 2025: 3 · 2024: 4 · 2023: 6 · 2022: 17 · 2021: 6 · 2020: 7 · 2019: 2
- FWCI
- 2.73
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- mediaTUM (Technical University of Munich) (submittedVersion, other-oa)
- Site cant be reached (submittedVersion, cc-by)
- Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) (submittedVersion, cc-by)
- Scopus (Elsevier) (submittedVersion, other-oa)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- Deutsche Forschungsgemeinschaft (SFB646, SFB1035, GRK1721, FOR1680, EXC114)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- RNA-binding proteins, RNA degradation, short linear motifs, unstructured regions, protein-protein interaction, RNA helicase
- MeSH terms
- Protein Domains, ATPases Associated with Diverse Cellular Activities, Amino Acid Sequence, Binding Sites, Carrier Proteins, Cell Nucleus, HeLa Cells, Humans, Mutation, Nuclear Proteins, Protein Binding, RNA-Binding Proteins, Sequence Homology, Amino Acid, Crystallography, X-Ray, RNA Helicases, Exosomes
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