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Fus deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death
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.
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“Fus-null mice die soon after birth179”
From The neurogenetics of alternative splicing (2016) · cites this paper as [179]
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Items 101–200 of 298
Hypomorphic mutation in hnRNP U results in post-implantation lethality
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“…Rangap1 (Ran GTPase activating protein) (DeGregori et al., 1994), EphA2 (Eph receptor A2) (Chen et al., 1996), Hnrpc (Williamson et al., 2000), Fus (Hicks et al., 2000) and Prmt1 (arginine methyltransferase 1) (Pawlak et al., 2000), as well as a hypomorphic allele involving Hnrpa2b1 (hnRNP A2/B1)…”
BackgroundSelf-citationUncovering the Role of RNA-Binding Proteins in Gene Expression in the Immune System
Díaz‐Muñoz, M. D., & Turner, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01094 · Cited by 79
“Expression of the splicing factors FUS, SC35, hnRPNPL, and hnRPNPLL is important for B- and T-cell development and for T-cell activation (128, 129).”
BackgroundHigelin, J., Demestre, M., Putz, S., Delling, J. P., Jacob, C., Lutz, A.-K., Bausinger, J., Huber, A., Klingenstein, M., Barbi, G., et al. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00290 · Cited by 82
“KO FUS mice die at birth and show genomic Frontiers in Cellular Neuroscience | www.frontiersin.org 17 December 2016 | Volume 10 | Article 290 instability (Hicks et al., 2000) and fibroblasts derived from these mice are very sensitive to radiation (Hicks et al., 2000; Kuroda et al., 2000).”
BackgroundSynaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic Functions
Ling, S. (2018) · Neural Plasticity · doi:10.1155/2018/8413496 · Cited by 85
FUS/TLS Is a Novel Mediator of Androgen-Dependent Cell-Cycle Progression and Prostate Cancer Growth
Brooke, G. N., Culley, R. L., Dart, D. A., Mann, D. J., Gaughan, L., McCracken, S. R., Robson, C. N., Spencer‐Dene, B., Gamble, S. C., Powell, S. M., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0874 · Cited by 79
“FUS is a multifunctional protein, being implicated in pre-mRNA splicing (9), chromosome stability (10), cell spreading (11), and transcription (12, 13).”
BackgroundGenome-wide analysis of microRNA and mRNA expression signatures in cancer
Li, M., Fu, S., & Xiao, H. (2015) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.67 · Cited by 80
Conjoint pathologic cascades mediated by ALS/FTLD-U linked RNA-binding proteins TDP-43 and FUS
Ito, D., & Suzuki, N. (2011) · Neurology · doi:10.1212/wnl.0b013e3182343365 · Cited by 78
Comprehensive gene expression profile of human activated Th1- and Th2-polarized cells
Nagai, S., Hashimoto, S.-I., Yamashita, T., Toyoda, N., Satoh, T., Suzuki, T., & Matsushima, K. (2001) · International Immunology · doi:10.1093/intimm/13.3.367 · Cited by 75
Sasayama, H., Shimamura, M., Tokuda, T., Azuma, Y., Yoshida, T., Mizuno, T., Nakagawa, M., Fujikake, N., Nagai, Y., & Yamaguchi, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039483 · Cited by 80
“FUS knockout mice show perinatal lethality and defects in B lymphocyte development [51].”
BackgroundFET family fusion oncoproteins target the SWI/SNF chromatin remodeling complex
Lindén, M., Thomsen, C., Grundevik, P., Jonasson, E., Andersson, D., Runnberg, R., Dolatabadi, S., Vannas, C., Santamaría, M. L., Fagman, H., et al. (2019) · EMBO Reports · doi:10.15252/embr.201845766 · Cited by 74
“Normal FET proteins shuttle between nucleus and cytoplasm, whereas the fusion oncoproteins are mainly restricted to the nuclei [5,36,37].”
Phenotypes and malignancy risk of different FUS mutations in genetic amyotrophic lateral sclerosis
Naumann, M., Peikert, K., Günther, R., van der Kooi, A. J., Aronica, E., Hübers, A., Danel-Brunaud, V., Corcia, P., Pan-Montojo, F. J., Çırak, S., et al. (2019) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.50930 · Cited by 77
“The fact that FUS knock-out mouse embryonic fibroblasts display abundant chromosomal instability and enhanced radiation sensitivity would underline this reasoning.(16,17) Neurodegenerative diseases in general were reported to correlate with an altered risk for malignant diseases.”
BackgroundSynaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS
Sahadevan, S., Hembach, K., Tantardini, E., Pérez‐Berlanga, M., Hruška-Plocháň, M., Megat, S., Weber, J., Schwarz, P., Dupuis, L., Robinson, M. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23188-8 · Cited by 77
Renoux, A. J., & Todd, P. K. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.10.006 · Cited by 75
Highly Efficient Targeted Mutagenesis in Mice Using TALENs
Panda, S. K., Wefers, B., Ortiz, O., Floß, T., Schmid, B., Haass, C., Wurst, W., & Kühn, R. (2013) · Genetics · doi:10.1534/genetics.113.156570 · Cited by 71
Role of Ionizing Radiation in Neurodegenerative Diseases
Sharma, N. K., Sharma, R., Mathur, D., Sharad, S., Minhas, G., Bhatia, K., Anand, A., & Ghosh, S. P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00134 · Cited by 75
“The knock-out of the FUS gene in different studies has revealed aberrant DNA repair machinery and hence, sensitivity toward radiation exposure (Hicks et al., 2000; Kuroda et al., 2000).”
BackgroundAkhmedov, A. T. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.16.3022 · Cited by 71
TDP‐43 and FUS/TLS: cellular functions and implications for neurodegeneration
Fiesel, F. C., & Kahle, P. J. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08258.x · Cited by 69
Fecto, F., & Siddique, T. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9637-9 · Cited by 71
“In fact, a previous study had already demonstrated that FUS deficiency leads to perinatal death in mice, whereas hemizygous mice appear to have a normal phenotype (Hicks et al. 2000).”
BackgroundCozzolino, M., Pesaresi, M. G., Gerbino, V., Großkreutz, J., & Carrı̀, M. T. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4328 · Cited by 66
Genetic Rodent Models of Amyotrophic Lateral Sclerosis
Bosch, L. V. D. (2011) · BioMed Research International · doi:10.1155/2011/348765 · Cited by 70
“ALS6 FUS/TLS Dominant (recessive) Mouse FUS/TLS KO [40, 41]”
FUS-related proteinopathies: Lessons from animal models
Lanson, N. A., & Pandey, U. B. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.039 · Cited by 66
Huang, C., Tong, J., Bi, F., Wu, Q., Huang, B., Zhou, H., & Xia, X. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds299 · Cited by 67
“FUS deficiency causes early death in homogeneous C57/BL6 background (27), but causes only male infertility in heterogeneous genomic background (28).”
BackgroundProteinopathies, neurodegenerative disorders with protein aggregation-based pathology
Shelkovnikova, T. A., Kulikova, A. A., Tsvetkov, P. O., Peters, O. M., Бачурин, С. О., Buchman, V. L., & Ninkina, N. N. (2012) · Molecular Biology · doi:10.1134/s0026893312020161 · Cited by 63
Gelon, P. A., Dutchak, P. A., & Sephton, C. F. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1000183 · Cited by 64
Beesley, A. H., Cummings, A. J., Freitas, J. R., Hoffmann, K., Firth, M. J., Ford, J., de Klerk, N. H., & Kees, U. R. (2005) · British Journal of Haematology · doi:10.1111/j.1365-2141.2005.05785.x · Cited by 59
“FUS is itself involved with multiple chromosomal translocations, has been identified as a marker of metastasis (Oue et al, 2004), and appears to be important for both B-lymphocyte development and the maintenance of genomic stability (Hicks et al, 2000).”
BackgroundSukhanova, M. V., Singatulina, A. S., Pastré, D., & Lavrik, O. I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197020 · Cited by 56
Post-transcriptional mechanisms in BCR/ABL leukemogenesis: role of shuttling RNA-binding proteins
Perrotti, D., & Calabretta, B. (2002) · Oncogene · doi:10.1038/sj.onc.1206085 · Cited by 55
“We favor the second possibility because: (i) a knock-out study showed that FUS null mice have an increased number of granulocytes (Hicks et al., 2000); and (ii) granulocytic differentiation is accelerated in myeloid precursor cells expressing FUS antisense transcripts (Perrotti et al., 1998).”
ResultAmyotrophic lateral sclerosis: an update on recent genetic insights
Iguchi, Y., Katsuno, M., Ikenaka, K., Ishigaki, S., & Sobue, G. (2013) · Journal of Neurology · doi:10.1007/s00415-013-7112-y · Cited by 56
“By contrast, FUS knockout mice on an inbred C57BL/6 background display perinatal death and exhibit abnormal lymphocytes and chromosomal instability [56], whereas knockout mice on an outbred background develop male sterility and survive until adulthood [57].”
BackgroundSpahn, L., Petermann, R., Siligan, C., Schmid, J. A., Aryee, D. N. T., & Kovar, H. (2002) · PubMed · Cited by 52
RNA Granules and Diseases: A Case Study of Stress Granules in ALS and FTLD
Fan, A. C., & Leung, A. K. L. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-29073-7_11 · Cited by 57
“Transgenic mice homozygous for an inactive FUS allele, for example, fail to suckle and die soon after birth (Hicks et al. 2000).”
BackgroundA loss of FUS/TLS function leads to impaired cellular proliferation
Ward, C. L., Boggio, K. J., Johnson, B. N., Boyd, J. D., Douthwright, S., Shaffer, S. A., Landers, J. E., Glicksman, M. A., & Bosco, D. A. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.508 · Cited by 52
RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insights
Rummens, J., & Cruz, S. D. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00851-y · Cited by 62
“As a result, global FUS knock-out in inbred mice causes perinatal lethality [403], highlighting its important role in development, and FUS depletion has been associated with synaptic defects in multiple in vitro and in vivo experimental model systems [401, 402, 404, 405].”
Sotoca, A. M., Prange, K. H. M., Reijnders, B., Mandoli, A., Nguyen, L. N. M., Stunnenberg, H. G., & Martens, J. H. A. (2015) · Oncogene · doi:10.1038/onc.2015.261 · Cited by 51
Sustained Expression of TDP-43 and FUS in Motor Neurons in Rodent's Lifetime
Huang, C., Xia, P. Y., & Zhou, H. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.396 · Cited by 51
“Expression patterns of the TDP-43 and FUS genes may explain why deletion of the TDP-43 or the FUS gene causes arrest to mouse development [6-8, 39, 40].”
BackgroundDNA Double-Strand Breaks as Pathogenic Lesions in Neurological Disorders
Provasek, V. E., Mitra, J., Malojirao, V. H., & Hegde, M. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094653 · Cited by 54
“instability and sensitization to IR [123,124].”
FUS-mediated alternative splicing in the nervous system: consequences for ALS and FTLD
Orozco, D., & Edbauer, D. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1077-2 · Cited by 52
“Inbred knockout mice fail to suckle and die within a few hours after birth [24].”
BackgroundPromoter-Associated Long Noncoding RNAs Repress Transcription Through a RNA Binding Protein TLS
Kurokawa, R. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0332-6_12 · Cited by 52
Funikov, S. Y., Rezvykh, A. P., Mazin, P., Morozov, A. V., Maltsev, A. V., Chicheva, M. M., Vikhareva, E. A., Евгеньев, М. Б., & Ustyugov, A. A. (2018) · Neurogenetics · doi:10.1007/s10048-018-0553-9 · Cited by 53
Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity
Oh, S.-M., Liu, Z., Okada, M., Jang, S.-W., Liu, X., Chan, C.-B., Luo, H., & Ye, K.-N. (2009) · Oncogene · doi:10.1038/onc.2009.411 · Cited by 47
“TLS deficiency in mice results in defective B-lymphocyte development and activation, high levels of chromosomal instability and perinatal death (Hicks et al., 2000).”
BackgroundThe FUS gene is dual-coding with both proteins contributing to FUS-mediated toxicity
Brunet, M. A., Jacques, J., Nassari, S., Tyzack, G. E., McGoldrick, P., Zinman, L. H., Jean, S., Robertson, J., Patani, R., & Roucou, X. (2020) · EMBO Reports · doi:10.15252/embr.202050640 · Cited by 56
Klaric, J. A., Wüst, S., & Panier, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.668821 · Cited by 46
Promoter-Associated Noncoding RNA from the CCND1 Promoter
Song, X., Wang, X., Arai, S., & Kurokawa, R. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-376-9_39 · Cited by 45
fus/TLS orchestrates splicing of developmental regulators during gastrulationPreprint
Dichmann, D. S., & Harland, R. M. (2012) · Genes & Development · doi:10.1101/gad.187278.112 · Cited by 45
“In a mouse gene trap screen, a Fus mutant with an insertion in exon 12 suffered perinatal death, possibly due to lymphocyte defects and chromosomal instability (Hicks et al. 2000).”
BackgroundThomsen, C., Grundevik, P., Elias, P., Ståhlberg, A., & Åman, P. (2013) · The FASEB Journal · doi:10.1096/fj.13-234435 · Cited by 45
Insulin-like growth factor 1 in diabetic neuropathy and amyotrophic lateral sclerosis
Rauskolb, S., Dombert, B., & Sendtner, M. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.04.007 · Cited by 45
Guipaud, O., Guillonneau, F., Labas, V., Praseuth, D., Rossier, J., López, B. S., & Bertrand, P. (2006) · PROTEOMICS · doi:10.1002/pmic.200600259 · Cited by 42
Steyaert, J., Scheveneels, W., Vanneste, J., Damme, P. V., Robberecht, W., Callaerts, P., Bogaert, E., & Bosch, L. V. D. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy303 · Cited by 42
“models showed an increase in aneuploidy and chromosomal aberrations in affected cells, highlighting the importance of FUS in genomic maintenance and chromosomal stability (43).”
BackgroundModelling amyotrophic lateral sclerosis in rodents
Todd, T. W., & Petrucelli, L. (2022) · Nature reviews. Neuroscience · doi:10.1038/s41583-022-00564-x · Cited by 44
FUS-regulated RNA metabolism and DNA damage repair
Zhou, Y., Liu, S., Öztürk, A., & Hicks, G. G. (2014) · Rare Diseases · doi:10.4161/rdis.29515 · Cited by 50
“We and others have demonstrated that FUS is required for DNA damage repair.(14,15,17) FUS is involved in DNA double strand break repair including both homologous recombination (HR) and non-homologous end joining repair (NHEJ) pathways.”
InfluentialSelf-citationRNA binding proteins: a common denominator of neuronal function and dysfunction
Doxakis, E. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-014-1443-7 · Cited by 40
“Inbred fus-null mice die perinatally([91]) and exhibit dendritic spine defects compatible with its role in local mRNA transport([92]) and translation([92]).”
BackgroundPelletier, S. W., Gingras, S., Howell, S. R., Vogel, P., & Ihle, J. N. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1787-12.2012 · Cited by 39
“Instead, targeted deletion of causative genes in mice most often results in early embryonic lethality, likely because of their wide, often ubiquitous, expression and the fundamental functions they perform within cells (Hicks et al., 2000; Sephton et al., 2009; Wu et al., 2009; Burgess et al., 2010).”
BackgroundFused in sarcoma/translocated in liposarcoma: A multifunctional DNA/RNA binding protein
Yang, S., Warraich, S. T., Nicholson, G. A., & Blair, I. P. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.06.003 · Cited by 36
Stem cell transplantation in neurological diseases: improving effectiveness in animal models
Adami, R., Scesa, G., & Bottai, D. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00017 · Cited by 38
“Recently, mice were developed with the mutation in the genes encoding the TAR DNA-binding protein 43 (Wegorzewska et al., 2009) and FUS/TLS (Hicks et al., 2000).”
BackgroundLaferrière, F., & Polymenidou, M. (2015) · Swiss Medical Weekly · doi:10.4414/smw.2015.14054 · Cited by 43
Amyotrophic Lateral Sclerosis, FUS and Protein Synthesis Defects
Assoni, A. F., Foijer, F., & Zatz, M. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10489-8 · Cited by 37
Schöpf, J., Uhrig, S., Heilig, C. E., Lee, K.-S., Walther, T., Carazzato, A., Dobberkau, A. M., Weichenhan, D., Plass, C., Hartmann, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44360-2 · Cited by 34
Markert, S. M., Skoruppa, M., Yu, B., Mulcahy, B., Zhen, M., Gao, S., Sendtner, M., & Stigloher, C. (2020) · Biology Open · doi:10.1242/bio.055129 · Cited by 34
“A reduction of protein translation might account for endosome and vesicle docking defects FUS has many functions related to DNA and RNA processing and maintenance (Ratti and Buratti, 2016), and knock-out leads to perinatal death in mice (Hicks et al., 2000).”
BackgroundColombrita, C., Onesto, E., Tiloca, C., Ticozzi, N., Silani, V., & Ratti, A. (2011) · PubMed · doi:10.4449/aib.v149i1.1261 · Cited by 32
Baloh, R. H. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a269b · Cited by 33
Modelling amyotrophic lateral sclerosis in mice
Stephenson, J., & Amor, S. (2017) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2018.10.001 · Cited by 34
Essential tremor: genetic update
Deng, H., Wu, S., & Jankovic, J. J. (2019) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2019.7 · Cited by 33
Functional characterization of a FUS mutant zebrafish line as a novel genetic model for ALS
Bourefis, A.-R., Campanari, M., Buée‐Scherrer, V., & Kabashi, E. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104935 · Cited by 35
“Fus mice were reported to die within 16 h of birth and affected cells were showing an increase in aneuploidy and chromosomal aberrations (Hicks et al., 2000).”
Kanazawa, T., Ogawa, C., Taketani, T., Taki, T., Hayashi, Y., & Morikawa, A. (2005) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190500162203 · Cited by 29
PGC-1α Regulates Translocated in Liposarcoma Activity: Role in Oxidative Stress Gene Expression
Sánchez‐Ramos, C., Tiérrez, A., Fabregat‐Andrés, Ó., Wild, B., Sánchez‐Cabo, F., Arduini, A., Dopazo, A., & Monsalve, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3643 · Cited by 29
“TLS knockout mice have unstable genomes as a result of chromosomal pairing defects and enhanced sensitivity to radiation (21, 27).”
FUsed in Sarcoma Is a Novel Regulator of Manganese Superoxide Dismutase Gene Transcription
Dhar, S. K., Zhang, J. Y., Gál, J., Xu, Y., Lu, M., Lynn, B. C., Zhu, H., Kasarskis, E. J., & Clair, D. K. S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4984 · Cited by 29
Status of ALS treatment, insights into therapeutic challenges and dilemmas
Khamaysa, M., & Pradat, P.-F. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12101601 · Cited by 28
Luo, Y., Blechingberg, J., Fernandes, A. M., Li, S., Fryland, T., Børglum, A. D., Bolund, L., & Nielsen, A. L. (2015) · BMC Genomics · doi:10.1186/s12864-015-2125-9 · Cited by 31
“FUS and EWS deficient mice and zebra fish show defects in DNA pairing and DNA repair [35–38] and the FET-proteins are able to pair homologous DNA in vitro [39–41].”
BackgroundLin, G., Mao, D., & Bellen, H. J. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.004 · Cited by 29
Hume, D. A., Sasmono, R. T., Himes, S. R., Sharma, S. M., Bronisz, A., Constantin, M., Ostrowski, M. C., & Ross, I. L. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.10.6733 · Cited by 28
“The authors claim there was no myeloid phenotype (28), but the data actually show that the number of monocytes in peripheral blood was substantially reduced.”
BackgroundGenetics of essential tremor: From phenotype to genes, insights from both human and mouse studies
Schmouth, J.-F., Dion, P. A., & Rouleau, G. A. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.05.001 · Cited by 27
“(2014), http://dx.doi.o indistinguishable from their wildtype littermates, whereas Fus / animals were slightly smaller in stature at birth; a phenomenon that appeared to be background dependent (Hicks et al., 2000; Kuroda et al., 2000).”
BackgroundMethodInfluentialOverexpression of nuclear FUS induces neuronal cell death
Suzuki, H., & Matsuoka, M. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.12.007 · Cited by 25
Martínez-Macías, M. I., Moore, D. A. Q., Green, R. L., Gómez-Herreros, F., Naumann, M., Hermann, A., Damme, P. V., Hafezparast, M., & Caldecott, K. W. (2019) · Life Science Alliance · doi:10.26508/lsa.201800222 · Cited by 28
“For example, FUS is phosphorylated by the DNA damage sensor protein kinases ATM and/or DNA-PK following treatment of cells with ionising radiation (IR) or etoposide (25, 26), and FUS de fi ciency in mice is associated with increased sensitivity to IR and elevated chromosome instability (27, 28).”
InfluentialWhy TDP-43? Why Not? Mechanisms of Metabolic Dysfunction in Amyotrophic Lateral Sclerosis
Floare, M.-L., & Allen, S. P. (2020) · Neuroscience Insights · doi:10.1177/2633105520957302 · Cited by 25
The EWS protein is dispensable for Ewing tumor growth.
Kovar, H., Jug, G., Hattinger, C. M., Spahn, L., Aryee, D. N. T., Ambros, P. F., Zoubek, A., & Gadner, H. (2001) · PubMed · Cited by 24
Self-assembly of FUS through its low-complexity domain contributes to neurodegeneration
Matsumoto, T., Matsukawa, K., Watanabe, N., Kishino, Y., Kunugi, H., Ihara, R., Wakabayashi, T., Hashimoto, T., & Iwatsubo, T. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy046 · Cited by 23
“FUS deficiency in mice resulted in perinatal or early death before adulthood in the inbred background (14,15).”
BackgroundAntisense oligonucleotide therapies for Amyotrophic Lateral Sclerosis: Existing and emerging targets
Klim, J. R., Vance, C. A., & Scotter, E. L. (2019) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2019.03.009 · Cited by 27
The FUS protein: Physiological functions and a role in amyotrophic lateral sclerosis
Efimova, A. D., Овчинников, Р. К., Roman, A. Y., Maltsev, A. V., Grigoriev, V. V., Kovrazhkina, E. A., & Skvortsova, V. I. (2017) · Molecular Biology · doi:10.1134/s0026893317020091 · Cited by 26
“For a long time, the consequences of loss of FUS function were difficult to study in mouse models because of male sterility [15] and a lower viability of FUS knockout mice [16].”
BackgroundCharacterization of genetic loss-of-function of Fus in zebrafish
Lebedeva, S., Domingues, A. M. D. J., Butter, F., & Ketting, R. F. (2016) · RNA Biology · doi:10.1080/15476286.2016.1256532 · Cited by 24
Genetic architecture of motor neuron diseases
Chaudhary, R., Agarwal, V., Rehman, M., Kaushik, A. S., & Mishra, V. (2021) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2021.120099 · Cited by 24
RNA Dysregulation in Diseases of Motor Neurons
Ibrahim, F., Nakaya, T., & Mourelatos, Z. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130307 · Cited by 24
Kerk, S. Y., Bai, Y., Smith, J., Lalgudi, P. V., Hunt, C., Kuno, J., Nuara, J., Yang, T., Lanza, K., Chan, N., et al. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.01.004 · Cited by 26
“Proper microglial differentiation in the context of these mutations was not a given considering that FUS KO (Hicks et al., 2000) and homozygous P517L (the murine analog of P525L) knockin (Lyashchenko, 2015) mice die perinatally.”
BackgroundFUS/TLS acts as an aggregation-dependent modifier of polyglutamine disease model mice
Kino, Y., Washizu, C., Kurosawa, M., Yamada, M., Doi, H., Takumi, T., Adachi, H., Katsuno, M., Sobue, G., Hicks, G. G., et al. (2016) · Scientific Reports · doi:10.1038/srep35236 · Cited by 21
Self-citationCharacterization of a new brain‐specific isoform of the EWS oncoprotein
Melot, T., Dauphinot, L., Sévenet, N., Radvanyi, F., & Delattre, O. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02251.x · Cited by 21
Ewing Tumor Biology: Perspectives for Innovative Treatment Approaches
Kovar, H. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0081-0_4 · Cited by 21
Screening for the Biomarkers Associated with Myocardial Infarction by Bioinformatics Analysis
Zhang, G., Li, J., Sun, H., & Yang, G. (2019) · Journal of Computational Biology · doi:10.1089/cmb.2019.0180 · Cited by 20
“One study showed that FUS null mice had immune defects and died within 16 hours after birth (Hicks et al., 2000).”
Fused in sarcoma regulates DNA replication timing and kinetics
Jia, W., Kim, S. H., Scalf, M., Tonzi, P., Millikin, R. J., Guns, W. M., Liu, L., Mastrocola, A. S., Smith, L. M., Huang, T. T., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101049 · Cited by 21
FUS causes synaptic hyperexcitability in Drosophila dendritic arborization neurons
Machamer, J. B., Woolums, B. M., Fuller, G. G., & Lloyd, T. E. (2018) · Brain Research · doi:10.1016/j.brainres.2018.03.037 · Cited by 19
“, 2015); (4) induction of the DNA damage response (Hicks et al., 2000; Kuroda, 2000; Qiu et al., 2014; Wang et al., 2013), and (5) a combination of these pathomechanisms (Shang and Huang, 2016).”
BackgroundModelling FUSopathies: focus on protein aggregation
Shelkovnikova, T. A. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130212 · Cited by 17
Parakh, S., Perri, E. R., Vidal, M., Sultana, J. M., Shadfar, S., Mehta, P. M., Konopka, A., Thomas, C. J., Spencer, D. M. S., & Atkin, J. D. (2021) · Scientific Reports · doi:10.1038/s41598-021-96181-2 · Cited by 17
FET family proto-oncogene Fus contributes to self-renewal of hematopoietic stem cells
Sugawara, T., Oguro, H., Negishi, M., Morita, Y., Ichikawa, H., Iseki, T., Yokosuka, O., Nakauchi, H., & Iwama, A. (2010) · Experimental Hematology · doi:10.1016/j.exphem.2010.04.006 · Cited by 18
“C57BL/6 inbred mice, in which Fus had been inactivated by retroviral gene-trapping, died shortly after birth, and showed non-cell-autonomous defects in B-lymphocyte development, impaired proliferative responses of B cells to specific mitogenic stimuli, and chromosomal instability [21].”
BackgroundInfluentialTrends in Understanding the Pathological Roles of TDP-43 and FUS Proteins
Buratti, E. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51140-1_15 · Cited by 19
Exploring the alternative: Fish, flies and worms as preclinical models for ALS
Braems, E., Tziortzouda, P., & Bosch, L. V. D. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136041 · Cited by 20
Recent Advances in Molecular Pathobiology of Gastric Carcinoma
Yasui, W., Oue, N., Kitadai, Y., & Nakayama, H. (2006) · Springer eBooks · doi:10.1007/4-431-27713-7_3 · Cited by 16
“FUS is a tumor-associated fusion gene, especially in myxoid liposarcoma, and its possible role is supposed to be to regulate transcription and maintain chromosomal stability [59].”
BackgroundWu, J., Xiao, J., Bai, M., Shi, C., Xin, Y., Zhao, W., Gao, X., Yin, M., & Zhao, J. (2023) · Infection and Immunity · doi:10.1128/iai.00029-23 · Cited by 13
“The lack of Fus in mice could lead to defective B lymphocyte development and activation (37), implying that Tfh2 may play a role in promoting B cell activation, proliferation, and differentiation in E.”
BackgroundThe Fusion Oncogene FUS-CHOP Drives Sarcomagenesis of High-Grade Spindle Cell Sarcomas in Mice
Chen, M., Xu, E. S., Leisenring, N. H., Cardona, D. M., Luo, L., Ma, Y., Ventura, A., & Kirsch, D. G. (2019) · Sarcoma · doi:10.1155/2019/1340261 · Cited by 14
“FUS homozygous knockout mice are radiosensitive and exhibit genomic instability [14, 15].”
BackgroundPromise of Nucleic Acid Therapeutics for Amyotrophic Lateral Sclerosis
Ito, D. (2021) · Annals of Neurology · doi:10.1002/ana.26259 · Cited by 15
Jensen, B. K., McAvoy, K. J., Heinsinger, N. M., Lepore, A. C., Ilieva, H. S., Haeusler, A. R., Trotti, D., & Pasinelli, P. (2022) · Glia · doi:10.1002/glia.24183 · Cited by 14
“B-cells derived from FUS-deficient mice have been shown to have reduced responses to traditional B-cell activating stim- uli (Hicks et al., 2000).”
BackgroundThe function of FUS in neurodevelopment revealed by the brain and spinal cord organoids
Zou, H., Wang, J., Ma, G., Xu, M., Luo, F., Zhang, L., & Wang, W. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103771 · Cited by 14
Structure and function of FUS gene in prostate cancer
Ghanbarpanah, E., Kohanpour, M. A., Hosseini-Beheshti, F., Yari, L., & Keshvari, M. (2018) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.4149/bll_2018_118 · Cited by 14
“The FUS encodes a multi-functional protein that requires the pre-mRNA interconnections (18), has a stable chromosome (19), expands the cell (20), and transcribes (22, 21).”
BackgroundReview: Modelling the pathology and behaviour of frontotemporal dementia
Solomon, D. A., Mitchell, J. C., Salcher-Konrad, M.-T., Vance, C. A., & Mizielinska, S. (2018) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12536 · Cited by 16
Metadata
- 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.
- Venue
- Nature Genetics
- Published
- 2000-02
- Volume
- 24
- Issue
- 2
- Pages
- 175-179
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- 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
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