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
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.
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“Another ALS and FTLD gene, FUS156, is a widely expressed, predominantly nuclear RNA-binding protein176,177”
From The neurogenetics of alternative splicing (2016) · cites this paper as [177]
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Cites
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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
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The C-terminal domain of RNA polymerase II couples mRNA processing to transcription
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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-citationShuttling of pre-mRNA binding proteins between nucleus and cytoplasm
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RNA recognition: towards identifying determinants of specificity
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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
Metadata
- 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
- 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
- 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
- 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
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