Cited by 350RNA Research and SplicingNuclear Structure and FunctionSarcoma Diagnosis and Treatment

The DOI matches its Crossref record; 33 of the 36 references it cites were found in a registry or an index.

TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling

Zinszner, Helene, Sok, John, Immanuel, David, Yin, Yin, Ron, David·1997·Journal of Cell Science

Open this paper in CoChat — free account

Abstract

TLS, the product of a gene commonly translocated in liposarcomas (TLS), is prototypical of a newly identified class of nuclear proteins that contain a C-terminal domain with a distinct RNA recognition motif (RRM) surrounded by Arg-Gly-Gly (RGG) repeats. Its unique N terminus serves as an essential transforming domain for a number of fusion oncoproteins in human sarcomas and leukemias. In this study we use an in vivo UV crosslinking procedure to probe the interactions of TLS with RNA. TLS is found to bind RNA in vivo and the association of TLS with RNA is rapidly diminished by treating cells with transcriptional inhibitors. This suggests that the species bound by TLS turns over rapidly. Surprisingly, the RRM was found to be dispensable for RNA binding by TLS in vivo, suggesting that at any one time most of the interactions between TLS and RNA in the cell are not sequence specific. Analysis of inter specific heterokaryons formed between human and mouse or Xenopus cells revealed that TLS engages in rapid nucleocytoplasmic shuttling, a finding confirmed by the ability of anti-TLS antibodies to trap TLS when injected into the cytoplasm of HeLa cells. Cellular fractionation experiments suggest that TLS binds to RNA in both the nucleus and cytoplasm and support the hypothesis that TLS functions as a heterogeneous ribonuclear protein (hnRNP)-like chaperone of RNA. These findings are discussed in the context of the role altered forms of TLS play in cellular transformation.

Integrity signals

Registry

Crossref · 10.1242/jcs.110.15.1741

Cites

33 of 33 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Rapid detection of octamer binding proteins with ‘mini extracts’, prepared from a small number of cells
Schreiber, E. H., Matthias, P., Müller, M. M., & Schaffner, W. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.15.6419 · Cited by 4,179
Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours
Delattre, O., Zucman, J., Plougastel, B., Desmaze, C., Melot, T., Peter, M., Kovar, H., Joubert, I., de Jong, P., Rouleau, G., et al. (1992) · Nature · doi:10.1038/359162a0 · Cited by 1,907
Conserved Structures and Diversity of Functions of RNA-Binding Proteins
Burd, C. G., & Dreyfuss, G. (1994) · Science · doi:10.1126/science.8036511 · Cited by 1,886
Chromosomal translocations in human cancer
Rabbitts, T. H. (1994) · Nature · doi:10.1038/372143a0 · Cited by 1,497
Major nucleolar proteins shuttle between nucleus and cytoplasm
Borer, R. A., Lehner, C. F., Eppenberger, H. M., & Nigg, E. A. (1989) · Cell · doi:10.1016/0092-8674(89)90241-9 · Cited by 1,113
The C-terminal domain of RNA polymerase II couples mRNA processing to transcription
McCracken, S. A., Fong, N., Yankulov, K., Ballantyne, S. M., Pan, G., Greenblatt, J., Patterson, S. D., Wickens, M., & Bentley, D. L. (1997) · Nature · doi:10.1038/385357a0 · Cited by 925
Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma
Crozat, A., Åman, P., Mandahl, N., & Ron, D. (1993) · Nature · doi:10.1038/363640a0 · Cited by 897
Self-citation
Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
Piñol-Roma, S., & Dreyfuss, G. (1992) · Nature · doi:10.1038/355730a0 · Cited by 842
RNA recognition: towards identifying determinants of specificity
Kenan, D. J., Query, C. C., & Keene, J. D. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90088-d · Cited by 724
Ewing sarcoma 11;22 translocation produces a chimeric transcription factor that requires the DNA-binding domain encoded by FLI1 for transformation.
May, W. A., Gishizky, M. L., Lessnick, S. L., Lunsford, L. B., Lewis, B. C., Delattre, O., Zucman‐Rossi, J., Thomas, G. D., & Denny, C. T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.12.5752 · Cited by 576

Show all 36 references

Sorted by citations

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021
TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 1,012
The changing scene of amyotrophic lateral sclerosis
Robberecht, W., & Philips, T. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3430 · Cited by 957
ALS‐associated fused in sarcoma (FUS) mutations disrupt Transportin‐mediated nuclear import
Dormann, D., Rodde, R., Edbauer, D., Bentmann, E., Fischer, I., Hruscha, A., Than, M. E., Mackenzie, I. R. A., Capell, A., Schmid, B., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.143 · Cited by 836
Cell-free Formation of RNA Granules: Bound RNAs Identify Features and Components of Cellular Assemblies
Han, T. W., Kato, M., Xie, S., Wu, L. C., Mirzaei, H., Pei, J., Chen, M., Xie, Y., Allen, J. D., Xiao, G., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.016 · Cited by 773
ALS Genetics, Mechanisms, and Therapeutics: Where Are We Now?
Mejzini, R., Flynn, L. L., Pitout, I. L., Fletcher, S., Wilton, S. D., & Akkari, P. A. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01310 · Cited by 803
A new subtype of frontotemporal lobar degeneration with FUS pathology
Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
King, O. D., Gitler, A. D., & Shorter, J. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.016 · Cited by 654
Protein aggregation in amyotrophic lateral sclerosis
Blokhuis, A. M., Groen, E. J. N., Koppers, M., van den Berg, L. H., & Pasterkamp, R. J. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1125-6 · Cited by 607
Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
Bosco, D. A., Lemay, N., Ko, H. K., Zhou, H., Burke, C., Kwiatkowski, T. J., Sapp, P. C., McKenna-Yasek, D. M., Brown, R. H., & Hayward, L. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq335 · Cited by 537
Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS
Sun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 461
ALS Genetics: Gains, Losses, and Implications for Future Therapies
Kim, G., Gautier, O., Tassoni-Tsuchida, E., Ma, X. R., & Gitler, A. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.022 · Cited by 370
The role of FUS gene variants in neurodegenerative diseases
Deng, H., Gao, K., & Jankovic, J. J. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.78 · Cited by 371
The neurogenetics of alternative splicing
Vuong, C. K., Black, D. L., & Zheng, S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.27 · Cited by 340
Biology of EWS/ETS fusions in Ewing's family tumors
Arvand, A., & Denny, C. T. (2001) · Oncogene · doi:10.1038/sj.onc.1204598 · Cited by 350
The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
Andersson, M. K., Ståhlberg, A., Arvidsson, Y., Olofsson, A., Semb, H., Stenman, G., Nilsson, O., & Åman, P. (2008) · BMC Cell Biology · doi:10.1186/1471-2121-9-37 · Cited by 354
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
Pesiridis, G. S., Lee, V. M.-Y., & Trojanowski, J. Q. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp303 · Cited by 325
The RNA Binding Protein TLS Is Translocated to Dendritic Spines by mGluR5 Activation and Regulates Spine Morphology
Fujii, R., Okabe, S., Urushido, T., Inoue, K., Yoshimura, A., Tachibana, T., Nishikawa, T., Hicks, G. G., & Takumi, T. (2005) · Current Biology · doi:10.1016/j.cub.2005.01.058 · Cited by 322
FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
Neumann, M., Bentmann, E., Dormann, D., Jawaid, A., DeJesus‐Hernandez, M., Ansorge, O., Roeber, S., Kretzschmar, H. A., Muñoz, D. G., Kusaka, H., et al. (2011) · Brain · doi:10.1093/brain/awr201 · Cited by 314
The TET Family of Proteins: Functions and Roles in Disease
Tan, A. Y., & Manley, J. L. (2009) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjp025 · Cited by 282
The RNA-binding Protein Fused in Sarcoma (FUS) Functions Downstream of Poly(ADP-ribose) Polymerase (PARP) in Response to DNA Damage
Mastrocola, A. S., Kim, S. H., Trinh, A. T., Rodenkirch, L. A., & Tibbetts, R. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497974 · Cited by 280
Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease
Neumann, M., Roeber, S., Kretzschmar, H. A., Rademakers, R., Baker, M. C., & Mackenzie, I. R. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0581-5 · Cited by 257
FUS pathology in basophilic inclusion body disease
Muñoz, D. G., Neumann, M., Kusaka, H., Yokota, O., Ishihara, K., Terada, S., Kuroda, S., & Mackenzie, I. R. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0598-9 · Cited by 259
TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
Fujii, R., & Takumi, T. (2005) · Journal of Cell Science · doi:10.1242/jcs.02692 · Cited by 253
Male sterility and enhanced radiation sensitivity in TLS−/− mice
Kuroda, M., Sok, J., Webb, L., Baechtold, H., Urano, F., Yin, Y., Chung, P., de Rooij, D. G., Akhmedov, A., Ashley, T., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.3.453 · Cited by 248
Self-citation
FUS stimulates microRNA biogenesis by facilitating co‐transcriptional Drosha recruitment
Morlando, M., Modigliani, S. D., Torrelli, G., Rosa, A., Carlo, V. D., Caffarelli, E., & Bozzoni, I. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.319 · Cited by 241
Biochemical Properties and Biological Functions of FET Proteins
Schwartz, J. C., Cech, T. R., & Parker, R. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034325 · Cited by 236
ELAV protein HuA (HuR) can redistribute between nucleus and cytoplasm and is upregulated during serum stimulation and T cell activation
Atasoy, U., Watson, J., Patel, D., & Keene, J. D. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3145 · Cited by 185
SARS-CoV-2 requires cholesterol for viral entry and pathological syncytia formation
Sanders, D. W., Jumper, C. C., Ackerman, P. J., Bracha, D., Donlic, A., Kim, H., Kenney, D., Castello-Serrano, I., Suzuki, S., Tamura, T., et al. (2021) · eLife · doi:10.7554/elife.65962 · Cited by 224
Oncoprotein TLS Interacts with Serine-Arginine Proteins Involved in RNA Splicing
Yang, L., Embree, L. J., Tsai, S., & Hickstein, D. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27761 · Cited by 225
Review: An update on clinical, genetic and pathological aspects of frontotemporal lobar degenerations
Lashley, T., Rohrer, J. D., Mead, S., & Révész, T. (2015) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12250 · Cited by 234
Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
Gál, J., Zhang, J. Y., Kwinter, D. M., Zhai, J., Jia, H., Jia, J., & Zhu, H. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.06.010 · Cited by 216
Amyotrophic Lateral Sclerosis-associated Proteins TDP-43 and FUS/TLS Function in a Common Biochemical Complex to Co-regulate HDAC6 mRNA*
Kim, S. H., Shanware, N. P., Bowler, M. J., & Tibbetts, R. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154831 · Cited by 221
TDP-43 and FUS: a nuclear affair
Dormann, D., & Haass, C. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.05.002 · Cited by 222
ALS-Associated FUS Mutations Result in Compromised FUS Alternative Splicing and Autoregulation
Zhou, Y., Liu, S., Liu, G., Öztürk, A., & Hicks, G. G. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003895 · Cited by 223
Liposarcoma: Molecular Genetics and Therapeutics
Conyers, R. K., Young, S., & Thomas, D. M. (2010) · Sarcoma · doi:10.1155/2011/483154 · Cited by 219
FUS Transgenic Rats Develop the Phenotypes of Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration
Huang, C., Zhou, H., Tong, J., Chen, H., Liu, Y., Wang, D., Wei, X., & Xia, X. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002011 · Cited by 224
RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations
Daigle, J. G., Lanson, N. A., Smith, R. B., Casci, I., Maltare, A., Monaghan, J., Nichols, C. D., Kryndushkin, D. S., Shewmaker, F. P., & Pandey, U. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds526 · Cited by 205
A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43
Lanson, N. A., Maltare, A., King, H., Smith, R. B., Kim, J. H., Taylor, J. P., Lloyd, T. E., & Pandey, U. B. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr150 · Cited by 209
TLS, EWS and TAF15: a model for transcriptional integration of gene expression
Law, W. J. (2006) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/ell015 · Cited by 203
FUS Interacts with HSP60 to Promote Mitochondrial Damage
Deng, J., Yang, M., Chen, Y., Chen, X., Liu, J., Sun, S., Cheng, H., Li, Y., Bigio, E. H., Mesulam, M. M., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005357 · Cited by 188
Identification of an RNA Binding Specificity for the Potential Splicing Factor TLS
Lerga, A., Hallier, M., Delva, L., Orvain, C., Gallais, I., Marie, J., & Moreau-Gachelin, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008304200 · Cited by 193
Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation
Mackenzie, I. R. A., Ansorge, O., Strong, M., Bilbao, J., Zinman, L., Ang, L.-C., Baker, M., Stewart, H., Eisen, A., Rademakers, R., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0838-7 · Cited by 183
FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress
Sama, R. R. K., Ward, C. L., Kaushansky, L. J., Lemay, N., Ishigaki, S., Urano, F., & Bosco, D. A. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24395 · Cited by 178
EWS–ETS oncoproteins: The linchpins of Ewing tumors
Janknecht, R. (2005) · Gene · doi:10.1016/j.gene.2005.08.007 · Cited by 173
Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation
Baechtold, H., Kuroda, M., Sok, J. C., Ron, D., López, B. S., & Akhmedov, A. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34337 · Cited by 171
Self-citation
Domain Architectures and Characterization of an RNA-binding Protein, TLS
Iko, Y., Kodama, T. S., Kasai, N., Oyama, T., Morita, E. H., Muto, T., Okumura, M., Fujii, R., Takumi, T., Tate, S.-I., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408552200 · Cited by 168
Mutations of FUS gene in sporadic amyotrophic lateral sclerosis
Corrado, L., Bo, R. D., Castellotti, B., Ratti, A., Cereda, C., Penco, S., Sorarú, G., Carlomagno, Y., Ghezzi, S., Pensato, V., et al. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2009.071027 · Cited by 170
Distinct pathological subtypes of FTLD-FUS
Mackenzie, I. R., Muñoz, D. G., Kusaka, H., Yokota, O., Ishihara, K., Roeber, S., Kretzschmar, H. A., Cairns, N. J., & Neumann, M. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0764-0 · Cited by 176
TDP ‐43 and FUS en route from the nucleus to the cytoplasm
Ederle, H., & Dormann, D. (2017) · FEBS Letters · doi:10.1002/1873-3468.12646 · Cited by 172
Mutational analysis reveals the FUS homolog TAF15 as a candidate gene for familial amyotrophic lateral sclerosis
Ticozzi, N., Vance, C. A., LeClerc, A. L., Keagle, P. J., Glass, J. D., McKenna‐Yasek, D., Sapp, P. C., Silani, V., Bosco, D. A., Shaw, C. E., et al. (2011) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.31158 · Cited by 172
FUS is Phosphorylated by DNA-PK and Accumulates in the Cytoplasm after DNA Damage
Deng, Q., Holler, C. J., Taylor, G., Hudson, K. F., Watkins, W., Gearing, M., Ito, D., Murray, M. E., Dickson, D. W., Seyfried, N. T., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0172-14.2014 · Cited by 161
Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort
Ticozzi, N., Silani, V., LeClerc, A. L., Keagle, P. J., Gellera, C., Ratti, A., Taroni, F., Kwiatkowski, T. J., McKenna‐Yasek, D., Sapp, P. C., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181bbff05 · Cited by 163
Intranuclear Aggregation of Mutant FUS/TLS as a Molecular Pathomechanism of Amyotrophic Lateral Sclerosis
Nomura, T., Watanabe, S., Kaneko, K., Yamanaka, K., Nukina, N., & Furukawa, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.516492 · Cited by 160
Amyotrophic lateral sclerosis-linked FUS/TLS alters stress granule assembly and dynamics
Baron, D. M., Kaushansky, L. J., Ward, C. L., Sama, R. R. K., Chian, R.-J., Boggio, K. J., Quaresma, A. J. C., Nickerson, J. A., & Bosco, D. A. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-30 · Cited by 159
Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis
Shang, Y., & Huang, E. J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.036 · Cited by 164
ALS-associated mutations in FUS disrupt the axonal distribution and function of SMN
Groen, E. J. N., Fumoto, K., Blokhuis, A. M., Engelen-Lee, J.-Y., Zhou, Y., van den Heuvel, D. M. A., Koppers, M., van Diggelen, F., van Heest, J., Demmers, J., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt222 · Cited by 153
De novo truncating FUS gene mutation as a cause of sporadic amyotrophic lateral sclerosis
DeJesus‐Hernandez, M., Kocerha, J., Finch, N. A., Crook, R., Baker, M. C., Desaro, P., Johnston, A., Rutherford, N. J., Wojtas, A., Kennelly, K. D., et al. (2010) · Human Mutation · doi:10.1002/humu.21241 · Cited by 158
Ewing sarcoma gene EWS is essential for meiosis and B lymphocyte development
Li, K., Watford, W. T., Li, C., Parmelee, A., Bryant, M., Deng, C., O’Shea, J. J., & Lee, S. B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31222 · Cited by 146
Transcription-Dependent Nuclear-Cytoplasmic Trafficking Is Required for the Function of the von Hippel-Lindau Tumor Suppressor Protein
Lee, S., Neumann, M., Stearman, R. S., Stauber, R. H., Pause, A., Pavlakis, G. N., & Klausner, R. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1486 · Cited by 142
Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D2concept
Uversky, V. N. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.36 · Cited by 147
ALS mutant FUS proteins are recruited into stress granules in induced Pluripotent Stem Cells (iPSCs) derived motoneurons
Lenzi, J., Santis, R. D., de Turris, V., Morlando, M., Laneve, P., Calvo, A., Caliendo, V., Chiò, A., Rosa, A., & Bozzoni, I. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.020099 · Cited by 140
Novel FUS/TLS Mutations and Pathology in Familial and Sporadic Amyotrophic Lateral Sclerosis
Hewitt, C., Kirby, J., Highley, J. R., Hartley, J. A., Hibberd, R., Hollinger, H. C., Williams, T. L., Ince, P. G., McDermott, C. J., & Shaw, P. J. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.52 · Cited by 140
Fused in sarcoma (FUS): An oncogene goes awry in neurodegeneration
Dormann, D., & Haass, C. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.03.006 · Cited by 140
Dr. Jekyll and Mr. Hyde: The Two Faces of the FUS/EWS/TAF15 Protein Family
Kovar, H. (2010) · Sarcoma · doi:10.1155/2011/837474 · Cited by 139
TLS-ERG Leukemia Fusion Protein Inhibits RNA Splicing Mediated by Serine-Arginine Proteins
Yang, L., Embree, L. J., & Hickstein, D. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3345-3354.2000 · Cited by 130
Functions of FUS/TLS From DNA Repair to Stress Response: Implications for ALS
Sama, R. R. K., Ward, C. L., & Bosco, D. A. (2014) · ASN NEURO · doi:10.1177/1759091414544472 · Cited by 134
TLS/FUS, a pro‐oncogene involved in multiple chromosomal translocations, is a novel regulator of BCR/ABL‐mediated leukemogenesis
Perrotti, D., Bonatti, S., Trotta, R., Martinez, R., Skorski, T., Salomoni, P., Grassilli, E., Iozzo, R. V., Cooper, D. R., & Calabretta, B. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4442 · Cited by 128
Characterization of Two Evolutionarily Conserved, Alternatively Spliced Nuclear Phosphoproteins, NFAR-1 and -2, That Function in mRNA Processing and Interact with the Double-stranded RNA-dependent Protein Kinase, PKR
Saunders, L. R., Perkins, D. J., Balachandran, S., Michaels, R., Ford, R. J., Mayeda, A., & Barber, G. N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104207200 · Cited by 126
Fus gene mutations in familial and sporadic amyotrophic lateral sclerosis
Rademakers, R., Stewart, H. G., DeJesus‐Hernandez, M., Krieger, C., Graff‐Radford, N. R., Fabros, M., Briemberg, H., Cashman, N. R., Eisen, A., & Mackenzie, I. R. (2010) · Muscle & Nerve · doi:10.1002/mus.21665 · Cited by 126
Proteomic analysis of FUS interacting proteins provides insights into FUS function and its role in ALS
Kamelgarn, M., Chen, J., Kuang, L., Arenas, A., Zhai, J., Zhu, H., & Gál, J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.015 · Cited by 125
The Ewing's sarcoma gene product functions as a transcriptional activator.
Rossow, K. L., & Janknecht, R. (2001) · PubMed · Cited by 120
Minor intron splicing is regulated by FUS and affected by ALS‐associated FUS mutants
Reber, S., Stettler, J., Filosa, G., Colombo, M., Jutzi, D., Lenzken, S. C., Schweingruber, C., Bruggmann, R., Bachi, A., Barabino, S. M. L., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593791 · Cited by 124
RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells
Doi, H., Okamura, K., Bauer, P. O., Furukawa, Y., Shimizu, H., Kurosawa, M., Machida, Y., Miyazaki, H., Mitsui, K., Kuroiwa, Y., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705306200 · Cited by 119
hnRNP A1 Nucleocytoplasmic Shuttling Activity Is Required for Normal Myelopoiesis and BCR/ABL Leukemogenesis
Iervolino, A., Santilli, G., Trotta, R., Guerzoni, C., Cesi, V., Bergamaschi, A., Gambacorti-Passerini, C. B., Calabretta, B., & Perrotti, D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.7.2255-2266.2002 · Cited by 121
The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis
Bampton, A., Gittings, L. M., Fratta, P., Lashley, T., & Gatt, A. P. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02203-0 · Cited by 116
The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
Rhoads, S. N., Monahan, Z. T., Yee, D. S., & Shewmaker, F. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030886 · Cited by 113
Identification of Mammalian Proteins Cross-linked to DNA by Ionizing Radiation
Barker, S., Weinfeld, M., Zheng, J., Li, L., & Murray, D. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502477200 · Cited by 115
Identification and characterization of FUS/TLS as a new target of ATM
Gardiner, M., Toth, R., Vandermoere, F., Morrice, N. A., & Rouse, J. (2008) · Biochemical Journal · doi:10.1042/bj20081135 · Cited by 111
Fusion genes in solid tumors
Åman, P. (1999) · Seminars in Cancer Biology · doi:10.1006/scbi.1999.0130 · Cited by 110
Proto-oncoprotein tls/fus is associated to the nuclear matrix and complexed with splicing factors ptb, srm160, and sr proteins
Meißner, M., Lopato, S., Gotzmann, J., Sauermann, G., & Barta, A. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00046-0 · Cited by 109
Role of FET proteins in neurodegenerative disorders
Svetoni, F., Frisone, P., & Paronetto, M. P. (2016) · RNA Biology · doi:10.1080/15476286.2016.1211225 · Cited by 110
Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS
Lee, M., Ghosh, U., Thurber, K. R., Kato, M., & Tycko, R. (2020) · Nature Communications · doi:10.1038/s41467-020-19512-3 · Cited by 104
Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads
Belly, A., Moreau-Gachelin, F., Sadoul, R., & Goldberg, Y. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2004.12.071 · Cited by 107
The Transcriptional Repressor ZFM1 Interacts with and Modulates the Ability of EWS to Activate Transcription
Zhang, D., Paley, A. J., & Childs, G. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18086 · Cited by 109
The genetics of amyotrophic lateral sclerosis: current insights
Kirby, J., Sultan, A. A., Waller, R., & Heath, P. R. (2016) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s84956 · Cited by 119
Axonal transport defects are a common phenotype in Drosophila models of ALS
Baldwin, K. R., Godena, V. K., Hewitt, V. L., & Whitworth, A. J. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw105 · Cited by 111
Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy
Fushimi, K., Long, C., Jayaram, N., Chen, X., Li, L., & Wu, J. Y. (2011) · Protein & Cell · doi:10.1007/s13238-011-1014-5 · Cited by 104
The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
Koyuncu, S., Sáez, I., Lee, H. J., Gutiérrez-García, R., Pokrzywa, W., Fatima, A., Hoppe, T., & Vı́lchez, D. (2018) · Nature Communications · doi:10.1038/s41467-018-05320-3 · Cited by 105
Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effects
Halliday, G. M., Bigio, E. H., Cairns, N. J., Neumann, M., Mackenzie, I. R., & Mann, D. M. A. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1030-4 · Cited by 100
A fruitful endeavor: Modeling ALS in the fruit fly
Casci, I., & Pandey, U. B. (2014) · Brain Research · doi:10.1016/j.brainres.2014.09.064 · Cited by 102
Expression of human FUS protein in Drosophila leads to progressive neurodegeneration
Chen, Y., Yang, M., Deng, J., Chen, X., Ye, Y., Zhu, L., Liu, J., Ye, H., Shen, Y., Li, Y., et al. (2011) · Protein & Cell · doi:10.1007/s13238-011-1065-7 · Cited by 103
Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fus-mediated ALS
Xia, R., Liu, Y., Yang, L., Gál, J., Zhu, H., & Jia, J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-10 · Cited by 106
Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase
Farg, M. A., Soo, K. Y., Walker, A. K., Pham, H., Orian, J. M., Horne, M. K., Warraich, S. T., Williams, K. L., Blair, I. P., & Atkin, J. D. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.009 · Cited by 101
Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases
Chen, C., Ding, X., Akram, N., Xue, S., & Luo, S. (2019) · Molecules · doi:10.3390/molecules24081622 · Cited by 96
A cytoplasmic long noncoding RNA LINC00470 as a new AKT activator to mediate glioblastoma cell autophagy
Liu, C., Zhang, Y., She, X., Li, F., Li, P., Feng, J., Fu, H., Liu, Q., Liu, Q., Zhao, C., et al. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0619-z · Cited by 94
A comparative clinical, pathological, biochemical and genetic study of fused in sarcoma proteinopathies
Lashley, T., Rohrer, J. D., Bandopadhyay, R., Fry, C., Ahmed, Z., Isaacs, A. M., Brelstaff, J., Borroni, B., Warren, J. D., Troakes, C., et al. (2011) · Brain · doi:10.1093/brain/awr160 · Cited by 93
PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
Jobert, L., Argentini, M., & Tora, L. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.12.008 · Cited by 93
FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis
Kryndushkin, D. S., Wickner, R. B., & Shewmaker, F. P. (2011) · Protein & Cell · doi:10.1007/s13238-011-1525-0 · Cited by 89

Authors: Zinszner, H., Sok, J., Immanuel, D., Yin, Y., & Ron, D.
Affiliations: Skirball Institute of Biomolecular Medicine, the Departments of Medicine, Cell Biology and the Kaplan Cancer Center, NYU Medical Center, New York, NY 10016, USA
NYU Langone Health (US)
ORCID: Yin, Yin
Ron, David
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 1997-08-01
Volume: 110
Issue: 15
Pages: 1741-1750
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.110.15.1741
OpenAlex: W2115670698
Cited by: 350
References: 36
Citations by year: 2026: 2 · 2025: 12 · 2024: 5 · 2023: 14 · 2022: 17 · 2021: 19 · 2020: 22 · 2019: 13 · 2018: 21 · 2017: 14 · 2016: 18 · 2015: 15 · 2014: 18 · 2013: 17 · 2012: 29
FWCI: 1.90
Type: journal article
Language: en
Open access: closed
Licence: www.biologists.com/user-licence-1-1/ (vor)
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ca060945-09)
National Cancer Institute (CA-60945)
National Institute of General Medical Sciences (5T32GM07038)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Health Sciences › Medicine › Oncology › Sarcoma Diagnosis and Treatment
Keywords: TLS, RNA recognition motif, RNA binding, nucleocytoplasmic shuttling, fusion oncoproteins, cell transformation, transcription inhibitors, heterokaryons, UV crosslinking
MeSH terms: Animals, Cell Nucleus, Centrifugation, Density Gradient, Cytoplasm, Dactinomycin, HeLa Cells, Humans, Ribonucleoproteins, RNA, Ultraviolet Rays, Xenopus, RNA-Binding Proteins, Coculture Techniques, Nucleic Acid Synthesis Inhibitors, COS Cells, Heterogeneous-Nuclear Ribonucleoproteins, RNA-Binding Protein FUS, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks