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Self-Assembled FUS Binds Active Chromatin and Regulates Gene Transcription

Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) is a DNA/RNA binding protein and mutations in FUS cause a subset of familial ALS. Most ALS mutations are clustered in the C-terminal nuclear localization sequence of FUS and consequently lead to th... Full description

Main Author: Yang, Liuqing
Other Authors: Gal, Jozsef , Chen, Jing , Zhu, Haining
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: DOI: 10.1073/pnas.1414004111
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recordid: uky_soai_uknowledge_uky_edu_biochem_facpub_1062
title: Self-Assembled FUS Binds Active Chromatin and Regulates Gene Transcription
format: Article
creator:
  • Yang, Liuqing
  • Gal, Jozsef
  • Chen, Jing
  • Zhu, Haining
subjects:
  • Amyotrophic Lateral Sclerosis
  • Blotting
  • Western
  • Chromatin
  • Gene Expression Regulation
  • Humans
  • Inclusion Bodies
  • Mutation
  • RNA-Binding Protein Fus
  • Transcription
  • Genetic
  • Biochemistry, Biophysics, and Structural Biology
ispartof:
description: Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) is a DNA/RNA binding protein and mutations in FUS cause a subset of familial ALS. Most ALS mutations are clustered in the C-terminal nuclear localization sequence of FUS and consequently lead to the accumulation of protein inclusions in the cytoplasm. It remains debatable whether loss of FUS normal function in the nucleus or gain of toxic function in the cytoplasm plays a more critical role in the ALS etiology. Moreover, the physiological function of FUS in the nucleus remains to be fully understood. In this study, we found that a significant portion of nuclear FUS was bound to active chromatin and that the ALS mutations dramatically decreased FUS chromatin binding ability. Functionally, the chromatin binding is required for FUS transcription activation, but not for alternative splicing regulation. The N-terminal QGSY (glutamine-glycine-serine-tyrosine)-rich region (amino acids...
language: eng
source:
identifier: DOI: 10.1073/pnas.1414004111
fulltext: fulltext_linktorsrc
url: Link


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titleSelf-Assembled FUS Binds Active Chromatin and Regulates Gene Transcription
creatorYang, Liuqing ; Gal, Jozsef ; Chen, Jing ; Zhu, Haining
identifierDOI: 10.1073/pnas.1414004111
subjectAmyotrophic Lateral Sclerosis ; Blotting ; Western ; Chromatin ; Gene Expression Regulation ; Humans ; Inclusion Bodies ; Mutation ; RNA-Binding Protein Fus ; Transcription ; Genetic ; Biochemistry, Biophysics, and Structural Biology
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0Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) is a DNA/RNA binding protein and mutations in FUS cause a subset of familial ALS. Most ALS mutations are clustered in the C-terminal nuclear localization sequence of FUS and consequently lead to the accumulation of protein inclusions in the cytoplasm. It remains debatable whether loss of FUS normal function in the nucleus or gain of toxic function in the cytoplasm plays a more critical role in the ALS etiology. Moreover, the physiological function of FUS in the nucleus remains to be fully understood. In this study, we found that a significant portion of nuclear FUS was bound to active chromatin and that the ALS mutations dramatically decreased FUS chromatin binding ability. Functionally, the chromatin binding is required for FUS transcription activation, but not for alternative splicing regulation. The N-terminal QGSY (glutamine-glycine-serine-tyrosine)-rich region (amino acids...
1Published in Proceedings of the National Academy of Sciences of the United States of America, v. 111, no. 50, p. 17809-17814.
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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) is a DNA/RNA binding protein and mutations in FUS cause a subset of familial ALS. Most ALS mutations are clustered in the C-terminal nuclear localization sequence of FUS and consequently lead to the accumulation of protein inclusions in the cytoplasm. It remains debatable whether loss of FUS normal function in the nucleus or gain of toxic function in the cytoplasm plays a more critical role in the ALS etiology. Moreover, the physiological function of FUS in the nucleus remains to be fully understood. In this study, we found that a significant portion of nuclear FUS was bound to active chromatin and that the ALS mutations dramatically decreased FUS chromatin binding ability. Functionally, the chromatin binding is required for FUS transcription activation, but not for alternative splicing regulation. The N-terminal QGSY (glutamine-glycine-serine-tyrosine)-rich region (amino acids...

1

Published in Proceedings of the National Academy of Sciences of the United States of America, v. 111, no. 50, p. 17809-17814.

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1Blotting
2Western
3Chromatin
4Gene Expression Regulation
5Humans
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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) is a DNA/RNA binding protein and mutations in FUS cause a subset of familial ALS. Most ALS mutations are clustered in the C-terminal nuclear localization sequence of FUS and consequently lead to the accumulation of protein inclusions in the cytoplasm. It remains debatable whether loss of FUS normal function in the nucleus or gain of toxic function in the cytoplasm plays a more critical role in the ALS etiology. Moreover, the physiological function of FUS in the nucleus remains to be fully understood. In this study, we found that a significant portion of nuclear FUS was bound to active chromatin and that the ALS mutations dramatically decreased FUS chromatin binding ability. Functionally, the chromatin binding is required for FUS transcription activation, but not for alternative splicing regulation. The N-terminal QGSY (glutamine-glycine-serine-tyrosine)-rich region (amino acids...

1

Published in Proceedings of the National Academy of Sciences of the United States of America, v. 111, no. 50, p. 17809-17814.

doi10.1073/pnas.1414004111
urlhttps://uknowledge.uky.edu/biochem_facpub/63
oafree_for_read
volume111
issue50
pages17809-17814
issn00278424
eissn10916490
date2014-12-16