Cited by 352RNA Research and SplicingAmyotrophic Lateral Sclerosis ResearchRNA and protein synthesis mechanisms

RNA targets of wild-type and mutant FET family proteins

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Hoell, Jessica I, Larsson, Erik, Runge, Simon, Nusbaum, Jeffrey D, Duggimpudi, Sujitha, Farazi, Thalia A, Hafner, Markus, Borkhardt, Arndt +2 more·2011·Nature Structural & Molecular Biology

Abstract

FUS, EWSR1 and TAF15, constituting the FET protein family, are abundant, highly conserved RNA-binding proteins with important roles in oncogenesis and neuronal disease, yet their RNA targets and recognition elements are unknown. Using PAR-CLIP, we defined global RNA targets for all human FET proteins and two ALS-causing human FUS mutants. FET members showed similar binding profiles, whereas FUS mutants showed a drastically altered binding pattern, consistent with changes in subcellular localization.

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Crossref · 10.1038/nsmb.2163

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  • The only instance where an RNAcompete motif did not have a significant positive AUROC to at least one corresponding in vivo data set was FUS, with AUROC <0.5 against in vivo crosslinking data for FUS and TAF15.

    “We found only one instance in which the RNAcompete motif did not have a significant and positive AUROC to at least one corresponding in vivo data set: the RNAcompete motif for FUS produced an AUROC <0.5 when compared to in vivo crosslinking-based data for both FUS and its paralogue TAF15”

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Authors
Hoell, J. I., Larsson, E., Runge, S., Nusbaum, J. D., Duggimpudi, S., Farazi, T. A., Hafner, M., Borkhardt, A., Sander, C., & Tuschl, T.
Affiliations
  • Howard Hughes Medical Institute (US)
  • Memorial Sloan Kettering Cancer Center (US)
  • Heinrich Heine University Düsseldorf (DE)
Corresponding author
  • Sander, Chris
  • Tuschl, Thomas
Venue
Nature Structural & Molecular Biology
Published
2011-11-13
Volume
18
Issue
12
Pages
1428-1431
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2038438413
Cited by
350
References
15
Citations by year
2026: 9 · 2025: 10 · 2024: 17 · 2023: 18 · 2022: 21 · 2021: 29 · 2020: 26 · 2019: 16 · 2018: 22 · 2017: 22 · 2016: 32 · 2015: 29 · 2014: 29 · 2013: 30 · 2012: 39
FWCI
12.84
Type
journal article
Language
en
Open access
Locations
  • Nature Structural & Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Howard Hughes Medical Institute
  • National Institute of Mental Health (MH08442, R01MH080442)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
FUS, EWSR1, TAF15, RNA-binding proteins, RNA targets, amyotrophic lateral sclerosis, FUS mutations, subcellular localization, PAR-CLIP, RNA-protein interactions
MeSH terms
Amyotrophic Lateral Sclerosis, Base Sequence, Binding Sites, Calmodulin-Binding Proteins, Humans, Mutation, RNA, Messenger, Sequence Alignment, RNA-Binding Proteins, Sequence Analysis, DNA, RNA-Binding Protein FUS, RNA-Binding Protein EWS, TATA-Binding Protein Associated Factors, HEK293 Cells

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