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

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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

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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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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
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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
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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

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

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