FUS is phosphorylated by DNA-PK and accumulates in the cytoplasm after DNA damage
Abnormal cytoplasmic accumulation of Fused in Sarcoma (FUS) in neurons defines subtypes of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). FUS is a member of the FET protein family that includes Ewing's sarcoma (EWS) and TATA-binding protein-associated factor 2...
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| Published in: | The Journal of neuroscience Vol. 34; no. 23; p. 7802 |
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| Format: | Journal Article |
| Language: | English |
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04.06.2014
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| Abstract | Abnormal cytoplasmic accumulation of Fused in Sarcoma (FUS) in neurons defines subtypes of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). FUS is a member of the FET protein family that includes Ewing's sarcoma (EWS) and TATA-binding protein-associated factor 2N (TAF15). FET proteins are predominantly localized to the nucleus, where they bind RNA and DNA to modulate transcription, mRNA splicing, and DNA repair. In ALS cases with FUS inclusions (ALS-FUS), mutations in the FUS gene cause disease, whereas FTLD cases with FUS inclusions (FTLD-FUS) do not harbor FUS mutations. Notably, in FTLD-FUS, all FET proteins accumulate with their nuclear import receptor Transportin 1 (TRN1), in contrast ALS-FUS inclusions are exclusively positive for FUS. In the present study, we show that induction of DNA damage replicates several pathologic hallmarks of FTLD-FUS in immortalized human cells and primary human neurons and astrocytes. Treatment with the antibiotic calicheamicin γ1, which causes DNA double-strand breaks, leads to the cytoplasmic accumulation of FUS, TAF15, EWS, and TRN1. Moreover, cytoplasmic translocation of FUS is mediated by phosphorylation of its N terminus by the DNA-dependent protein kinase. Finally, we observed elevated levels of phospho-H2AX in FTLD-FUS brains, indicating that DNA damage occurs in patients. Together, our data reveal a novel regulatory mechanism for FUS localization in cells and suggest that DNA damage may contribute to the accumulation of FET proteins observed in human FTLD-FUS cases, but not in ALS-FUS. |
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| AbstractList | Abnormal cytoplasmic accumulation of Fused in Sarcoma (FUS) in neurons defines subtypes of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). FUS is a member of the FET protein family that includes Ewing's sarcoma (EWS) and TATA-binding protein-associated factor 2N (TAF15). FET proteins are predominantly localized to the nucleus, where they bind RNA and DNA to modulate transcription, mRNA splicing, and DNA repair. In ALS cases with FUS inclusions (ALS-FUS), mutations in the FUS gene cause disease, whereas FTLD cases with FUS inclusions (FTLD-FUS) do not harbor FUS mutations. Notably, in FTLD-FUS, all FET proteins accumulate with their nuclear import receptor Transportin 1 (TRN1), in contrast ALS-FUS inclusions are exclusively positive for FUS. In the present study, we show that induction of DNA damage replicates several pathologic hallmarks of FTLD-FUS in immortalized human cells and primary human neurons and astrocytes. Treatment with the antibiotic calicheamicin γ1, which causes DNA double-strand breaks, leads to the cytoplasmic accumulation of FUS, TAF15, EWS, and TRN1. Moreover, cytoplasmic translocation of FUS is mediated by phosphorylation of its N terminus by the DNA-dependent protein kinase. Finally, we observed elevated levels of phospho-H2AX in FTLD-FUS brains, indicating that DNA damage occurs in patients. Together, our data reveal a novel regulatory mechanism for FUS localization in cells and suggest that DNA damage may contribute to the accumulation of FET proteins observed in human FTLD-FUS cases, but not in ALS-FUS.Abnormal cytoplasmic accumulation of Fused in Sarcoma (FUS) in neurons defines subtypes of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). FUS is a member of the FET protein family that includes Ewing's sarcoma (EWS) and TATA-binding protein-associated factor 2N (TAF15). FET proteins are predominantly localized to the nucleus, where they bind RNA and DNA to modulate transcription, mRNA splicing, and DNA repair. In ALS cases with FUS inclusions (ALS-FUS), mutations in the FUS gene cause disease, whereas FTLD cases with FUS inclusions (FTLD-FUS) do not harbor FUS mutations. Notably, in FTLD-FUS, all FET proteins accumulate with their nuclear import receptor Transportin 1 (TRN1), in contrast ALS-FUS inclusions are exclusively positive for FUS. In the present study, we show that induction of DNA damage replicates several pathologic hallmarks of FTLD-FUS in immortalized human cells and primary human neurons and astrocytes. Treatment with the antibiotic calicheamicin γ1, which causes DNA double-strand breaks, leads to the cytoplasmic accumulation of FUS, TAF15, EWS, and TRN1. Moreover, cytoplasmic translocation of FUS is mediated by phosphorylation of its N terminus by the DNA-dependent protein kinase. Finally, we observed elevated levels of phospho-H2AX in FTLD-FUS brains, indicating that DNA damage occurs in patients. Together, our data reveal a novel regulatory mechanism for FUS localization in cells and suggest that DNA damage may contribute to the accumulation of FET proteins observed in human FTLD-FUS cases, but not in ALS-FUS. Abnormal cytoplasmic accumulation of Fused in Sarcoma (FUS) in neurons defines subtypes of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). FUS is a member of the FET protein family that includes Ewing's sarcoma (EWS) and TATA-binding protein-associated factor 2N (TAF15). FET proteins are predominantly localized to the nucleus, where they bind RNA and DNA to modulate transcription, mRNA splicing, and DNA repair. In ALS cases with FUS inclusions (ALS-FUS), mutations in the FUS gene cause disease, whereas FTLD cases with FUS inclusions (FTLD-FUS) do not harbor FUS mutations. Notably, in FTLD-FUS, all FET proteins accumulate with their nuclear import receptor Transportin 1 (TRN1), in contrast ALS-FUS inclusions are exclusively positive for FUS. In the present study, we show that induction of DNA damage replicates several pathologic hallmarks of FTLD-FUS in immortalized human cells and primary human neurons and astrocytes. Treatment with the antibiotic calicheamicin γ1, which causes DNA double-strand breaks, leads to the cytoplasmic accumulation of FUS, TAF15, EWS, and TRN1. Moreover, cytoplasmic translocation of FUS is mediated by phosphorylation of its N terminus by the DNA-dependent protein kinase. Finally, we observed elevated levels of phospho-H2AX in FTLD-FUS brains, indicating that DNA damage occurs in patients. Together, our data reveal a novel regulatory mechanism for FUS localization in cells and suggest that DNA damage may contribute to the accumulation of FET proteins observed in human FTLD-FUS cases, but not in ALS-FUS. |
| Author | Deng, Qiudong Seyfried, Nicholas T Watkins, William Taylor, Georgia Ito, Daisuke Murray, Melissa E Dickson, Dennis W Hudson, Kathryn F Gearing, Marla Holler, Christopher J Kukar, Thomas |
| Author_xml | – sequence: 1 givenname: Qiudong surname: Deng fullname: Deng, Qiudong organization: Department of Pharmacology – sequence: 2 givenname: Christopher J surname: Holler fullname: Holler, Christopher J organization: Department of Pharmacology – sequence: 3 givenname: Georgia surname: Taylor fullname: Taylor, Georgia organization: Department of Pharmacology – sequence: 4 givenname: Kathryn F surname: Hudson fullname: Hudson, Kathryn F organization: Department of Pharmacology – sequence: 5 givenname: William surname: Watkins fullname: Watkins, William organization: Department of Pharmacology – sequence: 6 givenname: Marla surname: Gearing fullname: Gearing, Marla organization: Department of Pathology, Center for Neurodegenerative Disease – sequence: 7 givenname: Daisuke surname: Ito fullname: Ito, Daisuke organization: Department of Neurology, School of Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan, and – sequence: 8 givenname: Melissa E surname: Murray fullname: Murray, Melissa E organization: Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224 – sequence: 9 givenname: Dennis W surname: Dickson fullname: Dickson, Dennis W organization: Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224 – sequence: 10 givenname: Nicholas T surname: Seyfried fullname: Seyfried, Nicholas T organization: Center for Neurodegenerative Disease, Department of Biochemistry, and Department of Neurology, Emory University, School of Medicine, Atlanta, Georgia 30322 – sequence: 11 givenname: Thomas surname: Kukar fullname: Kukar, Thomas email: Thomas.Kukar@emory.edu organization: Department of Pharmacology, Center for Neurodegenerative Disease, Department of Neurology, Emory University, School of Medicine, Atlanta, Georgia 30322, Thomas.Kukar@emory.edu |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24899704$$D View this record in MEDLINE/PubMed |
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| Keywords | Fused in Sarcoma (FUS) amyotrophic lateral sclerosis (ALS) phosphorylation DNA damage frontotemporal lobar degeneration (FTLD) cytoplasmic translocation |
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| SubjectTerms | Aminoglycosides - pharmacology Antibiotics, Antineoplastic - pharmacology Astrocytes - drug effects Astrocytes - metabolism Cells, Cultured Cytoplasm - drug effects Cytoplasm - metabolism DNA Damage - drug effects DNA Damage - physiology DNA-Activated Protein Kinase - metabolism Enediynes - pharmacology Frontotemporal Lobar Degeneration - metabolism Frontotemporal Lobar Degeneration - pathology Humans Immunoprecipitation Mutagens - pharmacology Mutation - genetics Neurons Nuclear Proteins - metabolism Phosphorylation - drug effects Receptors, Cytoplasmic and Nuclear - metabolism RNA-Binding Protein EWS - metabolism RNA-Binding Protein FUS - metabolism TATA-Binding Protein Associated Factors - metabolism |
| Title | FUS is phosphorylated by DNA-PK and accumulates in the cytoplasm after DNA damage |
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