Cited by 299DNA Repair MechanismsT-cell and B-cell ImmunologyGenomics and Chromatin Dynamics

The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.

Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death

Hicks, Geoffrey G., Singh, Nagendra, Nashabi, Abudi, Mai, Sabine, Bozek, Gracjan, Klewes, Ludger, Arapovic, Djula, White, Erica K., Koury, Mark J., Oltz, Eugene M., Van Kaer, Luc, Ruley, H. E.·2000·Nature Genetics

DOI 10.1038/72842

Open this paper in CoChat — free account

Abstract

The gene FUS (also known as TLS (for translocated in liposarcoma) and hnRNP P2) is translocated with the gene encoding the transcription factor ERG-1 in human myeloid leukaemias. Although the functions of wild-type FUS are unknown, the protein contains an RNA-recognition motif and is a component of nuclear riboprotein complexes. FUS resembles a transcription factor in that it binds DNA, contributes a transcriptional activation domain to the FUS-ERG oncoprotein and interacts with several transcription factors in vitro. To better understand FUS function in vivo, we examined the consequences of disrupting Fus in mice. Our results indicate that Fus is essential for viability of neonatal animals, influences lymphocyte development in a non-cell-intrinsic manner, has an intrinsic role in the proliferative responses of B cells to specific mitogenic stimuli and is required for the maintenance of genomic stability. The involvement of a nuclear riboprotein in these processes in vivo indicates that Fus is important in genome maintenance.

Integrity signals

Registry

Crossref · 10.1038/72842

Cites

31 of 31 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
Atm-Deficient Mice: A Paradigm of Ataxia Telangiectasia
Barlow, C., Hirotsune, S., Paylor, R. E., Liyanage, M., Eckhaus, M., Collins, F. S., Shiloh, Y., Crawley, J. N., Ried, T., Tagle, D. A., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)80086-0 · Cited by 1,465
Targeted disruption of ATM leads to growth retardation, chromosomal fragmentation during meiosis, immune defects, and thymic lymphoma.Preprint
Xu, Y., Ashley, T., Brainerd, E. E., Bronson, R. T., Meyn, M. S., & Baltimore, D. (1996) · Genes & Development · doi:10.1101/gad.10.19.2411 · Cited by 830
Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation
Baskaran, R., Wood, L. D., Whitaker, L. L., Canman, C. E., Morgan, S. E., Xu, Y., Barlow, C., Baltimore, D., Wynshaw-Boris, A. J., Kastan, M. B., et al. (1997) · Nature · doi:10.1038/387516a0 · Cited by 538
Interaction between ATM protein and c-Abl in response to DNA damage
Shafman, T. D., Khanna, K. K., Kedar, P. S., Spring, K. J., Kozlov, S., Yen, T. J., Hobson, K., Gatei, M. H., Zhang, N., Watters, D. J., et al. (1997) · Nature · doi:10.1038/387520a0 · Cited by 478
Dual roles of ATM in the cellular response to radiation and in cell growth control.Preprint
Xu, Y., & Baltimore, D. (1996) · Genes & Development · doi:10.1101/gad.10.19.2401 · Cited by 407
Cutting edge: activation of NK T cells by CD1d and alpha-galactosylceramide directs conventional T cells to the acquisition of a Th2 phenotype.
Singh, N., Hong, S., Scherer, D. C., Serizawa, I., Burdin, N., Kronenberg, M., Koezuka, Y., & Kaer, L. V. (1999) · PubMed · Cited by 358
Self-citation
Transitional B cells are the target of negative selection in the B cell compartment.
Carsetti, R., Köhler, G., & Lamers, M. C. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.181.6.2129 · Cited by 358
A human RNA polymerase II complex associated with SRB and DNA-repair proteins
Maldonado, E., Shiekhattar, R., Sheldon, M., Cho, H. K., Drapkin, R., Rickert, P., Lees, E. M., Anderson, C. W., Linn, S., & Reinberg, D. (1996) · Nature · doi:10.1038/381086a0 · Cited by 351
Mice homozygous for the ablm1 mutation show poor viability and depletion of selected B and T cell populations
Schwartzberg, P. L., Stall, A. M., Hardin, J. D., Bowdish, K. S., Humaran, T. J., Boast, S., Harbison, M. L., Robertson, E. J., & Goff, S. P. (1991) · Cell · doi:10.1016/0092-8674(91)90012-n · Cited by 351

Show all 31 references

Sorted by citations

Items 201–298 of 298

Белок FUS: физиологические функции и роль в развитии бокового амиотрофического склероза, "Молекулярная биология"
Efimova, A. D., Овчинников, Р. К., Roman, A. Y., Maltsev, A. V., Григорьев, В. В., Kovrazhkina, E. A., & Skvortsova, V. I. (2017) · Molecular Biology · doi:10.7868/s0026898417020094 · Cited by 13
FUS Negatively Regulates Kaposi’s Sarcoma-Associated Herpesvirus Gene Expression
Dunker, W., Song, Y., Zhao, Y., & Karijolich, J. J. (2018) · Viruses · doi:10.3390/v10070359 · Cited by 12
“FUS is an important regulator of B cell development and activation, and considering B cells are the main reservoir of KSHV latency, it will be interesting to determine how KSHV infection impacts the role of FUS in these processes [45].”
Background
Amyotrophic Lateral Sclerosis Risk Genes and Suppressor
Ponnusamy, K., Haider, S., Kumar, R., Malik, M. Z., Singh, M., Rachana, R., & Mani, S. (2022) · Current Gene Therapy · doi:10.2174/1566523223666221108113330 · Cited by 11
RGG boxes within the TET/FET family of RNA-binding proteins are functionally distinct
Chau, B. L., Ng, K. P., Li, K. K. C., & Lee, K. A. W. (2016) · Transcription · doi:10.1080/21541264.2016.1183071 · Cited by 11
“proteins in protein networks (9) and scaffolds (10) and accordingly have diverse normal (11-17) and abnormal biological roles (7, 18, 19).”
Background
Naphthalene exposure: Effects on gene expression and proliferation in human cord blood cells
Diodovich, C., Malerba, I., Bowe, G., Acquati, F., Bianchi, M. G., Taramelli, R., Parent‐Massin, D., & Gribaldo, L. (2003) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.10091 · Cited by 11
Brain region-specific synaptic function of FUS underlies the FTLD-linked behavioural disinhibition
Wang, J.-Y., Ma, G., Tang, X., Shi, Q., Yu, M.-C., Lou, M.-M., He, K., & Wang, W. (2022) · Brain · doi:10.1093/brain/awac411 · Cited by 9
Disease Modeling of Rare Neurological Disorders in Zebrafish
Son, M., Kim, D. Y., & Kim, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073946 · Cited by 12
“Affected cells showed increased aneuploidy and chromosomal aberrations [109].”
Background
Rethinking antisense oligonucleotide therapeutics for amyotrophic lateral sclerosis
Ito, D., & Okada, K. (2024) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.52234 · Cited by 10
Motor Neuron Disease
Siddique, T., Deng, H., & Ajroud‐Driss, S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00141-5 · Cited by 9
TLS-GFP cannot rescue mRNP formation near spines and spine phenotype in TLS-KO
Fujii, R., Grossenbacher‐Zinchuk, O., Jamari, I., Wang, Y., Zinchuk, V. S., & Takumi, T. (2008) · Neuroreport · doi:10.1097/wnr.0b013e32831bedb0 · Cited by 9
The gene trap resource: A treasure trove for hemopoiesis research
Forrai, A., & Robb, L. (2005) · Experimental Hematology · doi:10.1016/j.exphem.2005.03.016 · Cited by 9
Fecundity in ALS
Byrne, S., Heverin, M., Bede, P., Elamin, M., & Hardiman, O. M. (2014) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2013.865237 · Cited by 8
Mouse pigpen encodes a nuclear protein whose expression is developmentally regulated during craniofacial morphogenesis
Alappat, S. R., Zhang, M., Zhao, X., Alliegro, M. A., Alliegro, M. C., & Burdsal, C. A. (2003) · Developmental Dynamics · doi:10.1002/dvdy.10353 · Cited by 8
Functional characterization of
Baethge, D.-B. K., Olbertz, J.-H., der Mathematisch-Naturwissenschaftlichen, D., & Hecht, S. (2014) · Cited by 9
Exposure to endogenous and exogenous sex hormones and reproductive history influence prognosis in women with ALS
Deniselle, M. C. G., Bettini, M., Garrido, R. M., Meyer, M., Lara, A., Garay, L. I., Casas, S., Fulgenzi, E., Núñez, M., Rugiero, M. F., et al. (2023) · Muscle & Nerve · doi:10.1002/mus.27942 · Cited by 7
“Likewise, limited fertility is present in murine models with genetic mutations associated with ALS that can be explained by defective zygotic implantation, chromosomal instability or male sterility.(41,42) However, another plausible explanation could be a premature ovarian failure that would account not only for infer…”
Background
Dynamic changes in RNA–protein interactions and RNA secondary structure in mammalian erythropoiesis
Shan, M., Ji, X., Janssen, K. A., Silverman, I. M., Humenik, J., Garcia, B., Liebhaber, S. A., & Gregory, B. D. (2021) · Life Science Alliance · doi:10.26508/lsa.202000659 · Cited by 7
“FUS has been identified to contribute to the maintenance of hematopoietic stem cells and FUS-deficient mice also exhibit abnormal hematopoietic phenotypes such as decreased B cell numbers, although no erythropoietic specific phenotypes have been reported (43, 44).”
ALS-linked FUS mutants affect the localization of U7 snRNP and replication-dependent histone gene expression in human cells
Gadgil, A., Walczak, A., Stępień, A., Mechtersheimer, J., Nishimura, A. L., Shaw, C. E., Ruepp, M., & Raczyńska, K. D. (2021) · Scientific Reports · doi:10.1038/s41598-021-91453-3 · Cited by 7
Mutation of the ALS-/FTD-Associated RNA-Binding Protein FUS Affects Axonal Development
van Tartwijk, F. W., Wunderlich, L. C. S., Mela, I., Makarchuk, S., Jakobs, M. A., Qamar, S., Franze, K., Schierle, G. S. K., George‐Hyslop, P. S., Lin, J. Q., et al. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.2148-23.2024 · Cited by 6
“FUS is known to be essential for development from mouse studies: its knock-out results in perinatal lethality (Hicks et al., 2000) and splicing changes in the central nervous system (Humphrey et al., 2020), but postnatal knock-out does not cause motor neuron death (A. Sharma et al., 2016).”
Emerging connections: Poly(ADP-ribose), FET proteins and RNA in the regulation of DNA damage condensates
Lombardi, S., Zilocchi, M., Nicsanu, R., & Barabino, S. M. L. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103846 · Cited by 6
FUS-dependent microRNA deregulations identify TRIB2 as a druggable target for ALS motor neurons
Ho, W. Y., Chak, L.-L., Hor, J., Liu, F., Díaz-García, S., Chang, J., Sanford, E., Gómez-Rodríguez, M. J., Alagappan, D., Lim, S. M., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108152 · Cited by 7
Model Systems of Motor Neuron Diseases As a Platform for Studying Pathogenic Mechanisms and Searching for Therapeutic Agents
Valetdinova, K. R., Medvedev, S. P., & Zakian, S. M. (2015) · Acta Naturae · doi:10.32607/20758251-2015-7-1-19-36 · Cited by 6
The atypical RNA-binding protein Taf15 regulates dorsoanterior neural development through diverse mechanisms in Xenopus tropicalis
DeJong, C. S., Dichmann, D. S., Exner, C. R. T., Xu, Y., & Harland, R. M. (2021) · Development · doi:10.1242/dev.191619 · Cited by 6
Frontotemporal lobar degeneration: toward the end of conFUSion
Frank, S., & Tolnay, M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0602-4 · Cited by 6
“Significantly, FUS knock-out mice show perinatal mortality [10].”
Fused in sarcoma-amyotrophic lateral sclerosis as a novel member of DNA single strand break diseases with pure neurological phenotypes
Hermann, A., Naumann, M., & Laubenthal, J. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.286963 · Cited by 5
“The latter, however, fits to the data from FUS–/– mice which – in case of homozygous loss of function – do also show genomic instability with much more tissues being affected (Hicks et al., 2000).”
Result
The RNA-binding protein FUS/TLS interacts with SPO11 and PRDM9 and localize at meiotic recombination hotspots
Giannattasio, T., Testa, E., Palombo, R., Chellini, L., Franceschini, F., Crevenna, Á. H., Petkov, P. M., Paronetto, M. P., & Barchi, M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04744-5 · Cited by 5
“Unfortunately, the current available Fus knockout model dies at perinatal age [82], therefore, at present, direct testing of the hotspot positioning shift in the absence of Fus or Fus and Ewsr1 is not possible.”
Background
FUS ALS-causative mutations impact FUS autoregulation and the processing of RNA-binding proteins through intron retentionPreprint
Humphrey, J., Birsa, N., Milioto, C., Robaldo, D., Eberle, A. B., Kräuchi, R., Bentham, M. P., Ule, A. M., Jarvis, S., Bodo, C., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/567735 · Cited by 5
“…(Chiang et al. 2010; Iguchi et al. 2013; Wils et al. 2010; Shan et al. 2010; Wegorzewska et al. 2009; Barmada et al. 2010; Arnold et al. 2013; Hicks et al. 2000; Kino et al. 2015; Verbeeck et al. 2012; Mitchell et al. 2013; Shiihashi et al. 2016; Qiu et al. 2014; Sharma et al. 2016), the…”
Background
Emerging roles for heterogeneous ribonuclear proteins in normal and malignant B cells
Qureshi, Q., Audas, T. E., Morin, R. D., & Coyle, K. M. (2023) · Biochemistry and Cell Biology · doi:10.1139/bcb-2022-0332 · Cited by 4
Pathology and pathophysiology
Dickerson, B. C. (2015) · Cambridge University Press eBooks · doi:10.1017/cbo9781316091586.016 · Cited by 4
Fused in sarcoma regulates glutamate signaling and oxidative stress response
Wong, C.-H., Rahat, A., & Chang, H. C.-H. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.11.015 · Cited by 4
Discovering the connection between familial and sporadic amyotrophic lateral sclerosis: pathology trumps genetics
Fecto, F., Deng, H., & Siddique, T. (2010) · Future Neurology · doi:10.2217/fnl.10.47 · Cited by 4
Radiation-Induced Neurodegeneration
Zedde, M., & Pascarella, R. (2026) · Biomedicines · doi:10.3390/biomedicines14020357 · Cited by 4
“The FUS gene has also been studied concerning ALS and radiation sensitivity, with knockouts revealing defective DNA repair mechanisms [247,248].”
New developments in pre-clinical models of ALS to guide translation
Cock, L. D., Bercier, V., & Bosch, L. V. D. (2024) · International review of neurobiology · doi:10.1016/bs.irn.2024.04.008 · Cited by 3
Fus Expression Patterns in Developing Tooth
Kim, E., Lee, J., & Jung, H.-S. (2013) · Development & Reproduction · doi:10.12717/dr.2013.17.3.215 · Cited by 3
“In addition, Fus－/－ mice have diminished cellularity in their lymphoid organs (Hicks et al., 2000).”
Background
Prognostic value of FUS immunoexpression for Gleason patterns and prostatic adenocarcinoma progression
Hirth, C. G., Vasconcelos, G. R., Lima, M. V. A., da Cunha, M. D. P. S. S., Frederico, I. K. S., & Dornelas, C. A. (2021) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2021.151729 · Cited by 3
Functional Genomics of the Murine Immune System
Ruley, H. E. (2001) · Immunologic Research · doi:10.1385/ir:23:2-3:289 · Cited by 3
Self-citation
FUS-dependent liquid-liquid phase separation is an early event in double-strand break repairPreprint
Levone, B. R., Lenzken, S. C., Antonaci, M., Maiser, A., Rapp, A. W., Conte, F., Reber, S., Mechtersheimer, J., Ronchi, A. E., Mühlemann, O., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/798884v2 · Cited by 3
Basic Concepts and Emergent Disease Mechanisms of Amyotrophic Lateral Sclerosis
Sirozh, O., Sáez-Mas, A., Lafarga, V., & Fernández-Capetillo, Ó. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00266-2 · Cited by 3
RNA-binding proteins TDP-43 and FUS promote R-loop resolution and regulate transcription termination
Zhao, D. Y., Nabeel‐Shah, S., Ni, Z., Pu, S., Zhong, G., Schmitges, F. W., Braunschweig, U., Blencowe, B. J., & Greenblatt, J. F. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111348 · Cited by 2
Transient hypogammaglobulinemia of infancy may be associated with reduced switched memory B cells and del (16) (p11.2p12)
Ito, T., Iwamoto, S., Hirayama, M., Yamada, Y., & Azuma, E. (2021) · Clinical Case Reports · doi:10.1002/ccr3.3837 · Cited by 2
The Molecular Basis of Sarcoma
Lessnick, S. L., Kovar, H., & Houghton, P. J. (2011) · Sarcoma · doi:10.1155/2011/864130 · Cited by 2
Translocated in liposarcoma regulates the distribution and function of mammalian enabled, a modulator of actin dynamics
Sugiura, T., Matsuda, S., Kurosaka, S., Nakai, N., Fukumoto, K., Takahashi, T., Maruyama, H., Imaizumi, K., Matsumoto, M., & Takumi, T. (2016) · FEBS Journal · doi:10.1111/febs.13685 · Cited by 2
Undervalued and novel roles of heterogeneous nuclear ribonucleoproteins in autoimmune diseases: Resurgence as potential biomarkers and targets
Chen, K., Luo, M., Lv, Y., Luo, Z., & Yang, H. (2023) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1806 · Cited by 2
Mislocalization, aggregation formation and defect in proteolysis in ALS
Tsubota, A., Ichijo, H., & Homma, K. (2016) · AIMS molecular science · doi:10.3934/molsci.2016.2.246 · Cited by 2
“FUS knockout mice do not show neuronal defects [93,94].”
Zebrafish C9orf72 loss-of-function models of Amyotrophic Lateral Sclerosis and Frontotemporal Dementia
Rounding, N. (2018) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York) · Cited by 2
Regulation of transcription termination by FUS and TDP-43Preprint
Zhao, D. Y., Ni, Z., Pu, S., Zhong, G., Schmitges, F. W., Braunschweig, U., Blencowe, B. J., & Greenblatt, J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/788778 · Cited by 2
“buildup of transcription-associated DNA damage (52,68-72).”
Synaptic accumulation of FUS triggers age-dependent misregulation of inhibitory synapses in ALS-FUS micePreprint
Sahadevan, S., Hembach, K., Tantardini, E., Pérez‐Berlanga, M., Hruška-Plocháň, M., Weber, J., Schwarz, P., Dupuis, L., Robinson, M. D., Rossi, P. D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.10.136010 · Cited by 2
Rhabdomyosarcomas of Bone
Shah, A., & Folpe, A. L. (2025) · Surgical pathology clinics · doi:10.1016/j.path.2025.01.010 · Cited by 1
Granules Gone Rogue: Nuclear and Cytoplasmic Ribonucleoprotein Structures in Amyotrophic Lateral Sclerosis-Fused in Sarcoma (ALS-FUS) Pathology
Ahuja, V., Sahu, B., Khurana, S., Kumari, K., Ganguly, N. K., Gourie‐Devi, M., Verma, S., Dastidar, S. G., & Taneja, V. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05736-9 · Cited by 1
“Nota-bly, however, genetic ablation or knockdown of FUS led to modest developmental phenotypes rather than progressive MN loss, suggesting that loss-of-function alone does not recapitulate the full spectrum of ALS pathology [87–90].”
Animal Models for PD and ALS
Kuenstling, M. V., Szlachetka, A. M., & Mosley, R. L. (2013) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-1-4614-8794-4_34 · Cited by 1
Targeting sarcomas by proteomic approaches
Madoz‐Gúrpide, J. (2009) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200800229 · Cited by 1
“Significantly, the homologous DNA-pairing activity of TET proteins is supported by the phenotypes of deficient mice [24], suggesting a role in genome plasticity control.”
Background
Implicated Role of Liposarcoma Related Fusion Oncoprotein TLS-CHOP in the Dysregulation of Arginine-Specific Methylation through PRMT1
Fujimoto, K. (2013) · Cell Biology · doi:10.11648/j.cb.20130102.11 · Cited by 1
“TLS is a multifunctional protein, which regulates transcription, pre-mRNA splicing, DNA repair and homologous recombination [7-12].”
Background
Signaling advances from immunogenetics to immunogenomics.
Boothby, M. R. (2003) · Genome biology · doi:10.1186/gb-2003-4-12-239 · Cited by 1
“As an example of the early success and potential of this strategy of retroviral mutagenesis, a novel link was identified between the mouse FUS gene, chromosomal stability, and B-lymphoid proliferation [16].”
Mechanisms of Dendrite Degeneration in Amyotrophic Lateral Sclerosis
Lee, S., Shang, Y., & Huang, E. J. (2016) · Springer eBooks · doi:10.1007/978-4-431-56050-0_21 · Cited by 1
Rare and favorable prognosis of pediatric acute lymphoblastic leukemia with TLS-ERG fusion gene: Case report with long-term follow-up and review of literature
Li, S., Huang, W., Wu, Y., Xu, X., Liao, C., & Tang, Y. (2021) · Cancer Genetics · doi:10.1016/j.cancergen.2021.04.003 · Cited by 1
Soft tissue tumors: Liposarcoma: Myxoid liposarcoma
Sánchez‐Martín, M., González‐Herrero, I., & Sánchez-Garcı́a, I. (2011) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/38162 · Cited by 1
TDP-43 and FUS in Amyotrophic Lateral Sclerosis: From Animal Models to Disease Mechanisms
Ebstein, S. Y. (2017) · doi:10.7916/d8p84q5f · Cited by 1
FUS gene is dual-coding with both proteins united in FUS-mediated toxicityPreprint
Brunet, M. A., Jacques, J., Nassari, S., Tyzack, G. E., McGoldrick, P., Zinman, L. H., Jean, S., Robertson, J., Patani, R., & Roucou, X. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/848580 · Cited by 1
Concepts | No Membrane, No Problem: Cellular Organization by Biomolecular Condensates
Sang, C. C., Moore, G., & Lee, H. O. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00329-7 · Cited by 1
The genetics and spread of Amyotrophic Lateral Sclerosis
Jones, A. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University)
EWSR1 and FUS fusion genes in tumorigenesis
Möller, E. (2010) · Lund University Publications (Lund University)
FUS (fusion involved in t(12;16) in malignant liposarcoma)
Pérez-Mancera, P., & Sánchez-Garîa, I. (2011) · Atlas of Genetics and Cytogenetics in Oncology and Haematology · doi:10.4267/2042/38109
FET proteins in cancer and development
Andersson, M. K. (2009) · Gothenburg University Publications Electronic Archive (Gothenburg University)
MicroRNA regulation by the DNA and RNA binding proteins EWS and FUS
Fernandes, A. M. (2012) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
FUS Transgenic Rats Develop the Phenotypes of Amyotrophic Lateral Sclerosis and Frontotemporal
Huang, C., & Zhou, H. (2011)
Modelling C9orf72-linked frontotemporal dementia and amyotrophic lateral sclerosis
Ryan, S. (2015) · Research Explorer (The University of Manchester)
A survey of axonal transport function and motor behaviour in Drosophila models of amyotrophic lateral sclerosis
Baldwin, K. R. (2015) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)
Pathophysiologyand animal models of frontotemporal dementia
Warmus, B. A., & Roberson, E. D. (2015) · Cambridge University Press eBooks · doi:10.1017/cbo9781316091586.018
The role of ALS associated genes and c-Jun in neurodegeneration
Acosta‐Saltos, A. (2016) · UCL Discovery (University College London)
Molecular Pathology of Bone and Soft Tissue Tumors
Ordóñez, J. L., Osuna, D., Madoz‐Gúrpide, J., & de Álava, E. (2016) · Springer eBooks · doi:10.1007/978-1-59745-458-2_34
Análisis de la función de EWS-FLI1 en la patogenia del Sarcoma de Ewing
Martín, D. H. (2008) · Gredos (University of Salamanca) · doi:10.14201/gredos.55568
Stress-induced non-coding RNAs allosterically regulate TLS, a HAT-inhibitory RNA binding protein, to mediate transcriptional repression
Wang, X. (2007) · eScholarship (California Digital Library)
Study of the multifunctional nuclear scaffold protein. A kinase anchoring protein 95
López-Soop, G. (2017) · NORA - Norwegian Open Research Archives
Autonomous and motor disorders
Pietropaolo, S., Sluyter, F., & Crusio, W. E. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781107360556.005
Systems Biology of RNA-Binding Proteins in Amyotrophic Lateral Sclerosis
Kashav, T., & Kumar, V. (2018) · RNA technologies · doi:10.1007/978-3-319-92967-5_4
TLS–CHOP in Myxoid Liposarcoma
Ladanyi, M., & Antonescu, C. R. (2002) · Elsevier eBooks · doi:10.1016/b0-12-227555-1/00243-4
RNA-Binding Proteins and Translation in Neurodegenerative Disease
Duncan, K. E. (2020) · Oxford University Press eBooks · doi:10.1093/oxfordhb/9780190686307.013.25
RNA-Binding Protein TAF15 Suppresses Toxicity in a Yeast Model of FUS Proteinopathy
Hayden, E., Kebe, A., Chen, S., Chumley, A., Xia, C., El-Zein, W., Zhong, Q., & Ju, S. (2026) · Journal of Fungi · doi:10.3390/jof12050341
“…that deficiency of FUS in animals leads to a variety of issues including perinatal lethality, genomic instability and hippocampal vacuolation [67,68] and that depletion of Cabeza, the drosophila homolog of FUS, results in locomotor defects [69–71], bypassing FUS toxicity without affecting the…”
Astrocytic expression of ALS-causative mutant FUS leads to TNFα-dependent neurodegeneration in vivoPreprint
Jensen, B. K., McAvoy, K., Heinsinger, N. M., Lepore, A., Ilieva, H., Haeusler, A., Trotti, D., & Pasinelli, P. (2021) · bioRxiv · doi:10.1101/2021.11.23.469650
“B-cells derived from FUS-deficient mice have been shown to have reduced responses to traditional B-cell activating stimuli (Hicks et al., 2000).”
Background
Motor disorders
Gordon, D., & Talbot, K. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9781107360556.008
A função de proteínas associadas à Esclerose Lateral Amiotrófica em diferentes contextos celulares
Assoni, A. F. (2022) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.41.2022.tde-02082022-190632
FUSDelta14 mutation impairs normal brain development and causes systemic metabolic alterationsPreprint
Godoy-Corchuelo, J. M., Ali, Z., Martins-Bach, A. B., García-Toledo, I., Fernández-Beltrán, L. C., Nair, R., Spring, S., Nieman, B. J., Jiménez-Coca, I., Bains, R. S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.24.529858
“FUS is involved in DNA damage response and repair machinery (41), and complete KO causes perinatal lethality in mice (52).”
Background
Functional Properties of Phase Separation and Intranuclear Complex of FUS in the Pathogenesis of ALS/FTLD
Ishigaki, S. (2023) · Springer eBooks · doi:10.1007/978-981-99-4886-4_14
Physiological function of FUS: An RNA binding protein in motor neuron disease
Yang, L. (2015) · UKnowledge (University of Kentucky)
Approche physiologiques et pharmacologiques dans un modèle murin de la sclérose latérale amytrophique
Gerber, Y. N. (2011) · theses.fr (ABES) · doi:10.70675/4234ace7z72a4z4873z9ec5zc82a77a8cce9
The role of serotoninergic neurons in amyotrophic lateral sclerosis
Oussini, H. E. (2016) · theses.fr (ABES) · doi:10.70675/2431e8ddzd4e4z4710z81dcz14100daa6294
Conditional truncation of the FUS protein in mice : a new animal model of the ALS/FTD continuum
Scekic‐Zahirovic, J. (2016) · theses.fr (ABES) · doi:10.70675/6bed4f95z0a05z438fz937ez33f29f11923d
Rôle du muscle squelettique dans la Sclérose Latérale Amyotrophique : apport de modèles transgéniques conditionnels
Picchiarelli, G. (2018) · theses.fr (ABES) · doi:10.70675/0252f66fz38f9z46b6z8f3ez97b2f3467520 · Cited by 1
Implication des macrophages périphériques dans la Sclérose latérale Amyotrophique
Chiot, A. (2018) · theses.fr (ABES) · doi:10.70675/e3d90f5az237az4722zbff2z9c99590e826b
Novel FUS and CHCHD10 models to investigate pathogenic mechanisms in Amyotrophic Lateral Sclerosis
Bourefis, A.-R. (2019) · theses.fr (ABES) · doi:10.70675/45ab8515z9859z430fzb472z306dd61206c8
Étude de l'augmentation du trafic en surface des récepteurs P2X4 de l’ATP à l’aide de nouveaux modèles murins transgéniques : implications dans les processus mnésiques et la sclérose latérale amyotrophique
Bertin, É. (2019) · theses.fr (ABES) · doi:10.70675/5ca95ac9z583cz4a23z88c4z20ef189cda74
Génétique de la Sclérose Latérale Amyotrophique et rôle de la voie de SUMOylation dans l'agrégation de la protéine TDP-43
Maurel, C. (2018) · theses.fr (ABES) · doi:10.70675/06af88a8z908cz41aaz9b6dz8cbea6bde2a8
The link between PARP1-mediated signaling and RNA-binding protein FUS in response to DNA damage
Singatulina, A. (2019) · theses.fr (ABES) · doi:10.70675/bdd8c1b6z3cfcz4fd8z9277z39ed8983ee72
Caractérisations biochimiques des protéines à répétitions de dipeptides et de leurs assemblages
Brasseur, L. (2019) · theses.fr (ABES) · doi:10.70675/9c659bfdz83dez45e5za549z64f5d270b2f9
Analyses génétiques et fonctionnelles de nouveaux gènes incriminés dans la Sclérose Latérale Amyotrophique (SLA)
Teyssou, E. (2017) · theses.fr (ABES) · doi:10.70675/6b2c9ef9z3766z4be8z8030zea731dbce4f3
Comprendre et modéliser la Sclérose Latérale Amyotrophique à début précoce
Muratet, F. (2022) · theses.fr (ABES) · doi:10.70675/9a7778aaz88c7z40b1z92d3zaf5699b86a09
Memory dysfunctions and associated epigenetic and transcriptomic changes in an ALS/FTD mouse model linked to a FUS mutation
Tzeplaeff, L. (2021) · theses.fr (ABES) · doi:10.70675/74ab85c6zb499z4f04za73az6e876ac228ba
Quantitative MRI Measurements of The Brainstem and Spinal Cord in Predicting Motor and Respiratory Capacity in Amyotrophic Lateral Sclerosis
Khamaysa, M. (2023) · theses.fr (ABES) · doi:10.70675/4e78f41ezb3fcz4940z9dcczfebf233cdc2d
FUS modulates R-loops by functionally interacting with RNase H1
Dey, A., Das, R., & Uppal, S. (2026) · Human Cell · doi:10.1007/s13577-026-01399-9
“Consistent with this, FUS knockout mice exhibit neonatal lethality accompanied by severe genomic instability and chromosomal abnormalities [28].”

Authors: Hicks, G. G., Singh, N., Nashabi, A., Mai, S., Bozek, G., Klewes, L., Arapovic, D., White, E. K., Koury, M. J., Oltz, E. M., Van Kaer, L., & Ruley, H. E.
Affiliations: University of Manitoba (CA)
Howard Hughes Medical Institute (US)
Vanderbilt University (US)
Corresponding author: Hicks, Geoffrey G.
ORCID: Hicks, Geoffrey G.
Singh, Nagendra
Mai, Sabine
Koury, Mark J.
Oltz, Eugene M.
Venue: Nature Genetics
Publisher: Springer Science and Business Media LLC
Published: 2000-02
Volume: 24
Issue: 2
Pages: 175-179
ISSN: 1061-4036 (ISSN-L)
1546-1718
DOI: 10.1038/72842
OpenAlex: W2080964315
Cited by: 299
References: 31
Citations by year: 2026: 5 · 2025: 3 · 2024: 4 · 2023: 10 · 2022: 17 · 2021: 19 · 2020: 10 · 2019: 17 · 2018: 21 · 2017: 10 · 2016: 26 · 2015: 12 · 2014: 18 · 2013: 23 · 2012: 13
FWCI: 2.51
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Genetics (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (2r01hg000684-04a1)
National Human Genome Research Institute (R01HG00684)
National Cancer Institute (P30CA042014)
National Center for Research Resources (R01RR013166)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: FUS gene, TLS, B cell development, B cell activation, chromosomal instability, genome stability, perinatal lethality, nuclear ribonucleoprotein, transcription factors
MeSH terms: Animals, Animals, Newborn, B-Lymphocytes, Bone Marrow Cells, Chimera, Crosses, Genetic, Female, Genotype, Humans, Liver, Lymphocyte Activation, Male, Mice, Inbred C57BL, Ribonucleoproteins, Spleen, Restriction Mapping, RNA-Binding Proteins, Mice, Knockout, 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

Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death

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