FUS-NLS/Transportin 1 Complex Structure Provides Insights into the Nuclear Targeting Mechanism of FUS and the Implications in ALS
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{"title"=>"FUS-NLS/Transportin 1 Complex Structure Provides Insights into the Nuclear Targeting Mechanism of FUS and the Implications in ALS", "type"=>"journal", "authors"=>[{"first_name"=>"Chunyan", "last_name"=>"Niu", "scopus_author_id"=>"55386433000"}, {"first_name"=>"Jiayu", "last_name"=>"Zhang", "scopus_author_id"=>"53983300200"}, {"first_name"=>"Feng", "last_name"=>"Gao", "scopus_author_id"=>"36682161100"}, {"first_name"=>"Liuqing", "last_name"=>"Yang", "scopus_author_id"=>"55732915000"}, {"first_name"=>"Minze", "last_name"=>"Jia", "scopus_author_id"=>"35792151800"}, {"first_name"=>"Haining", "last_name"=>"Zhu", "scopus_author_id"=>"7404663416"}, {"first_name"=>"Weimin", "last_name"=>"Gong", "scopus_author_id"=>"7202258601"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"23056579", "doi"=>"10.1371/journal.pone.0047056", "sgr"=>"84867290759", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "scopus"=>"2-s2.0-84867290759", "issn"=>"19326203", "pui"=>"365821722"}, "id"=>"0a9b0952-67dd-3fd4-bcc2-c4a34e508887", "abstract"=>"The C-terminal nuclear localization sequence of FUsed in Sarcoma (FUS-NLS) is critical for its nuclear import mediated by transportin (Trn1). Familial amyotrophic lateral sclerosis (ALS) related mutations are clustered in FUS-NLS. We report here the structural, biochemical and cell biological characterization of the FUS-NLS and its clinical implications. The crystal structure of the FUS-NLS/Trn1 complex shows extensive contacts between the two proteins and a unique α-helical structure in the FUS-NLS. The binding affinity between Trn1 and FUS-NLS (wide-type and 12 ALS-associated mutants) was determined. As compared to the wide-type FUS-NLS (K(D) = 1.7 nM), each ALS-associated mutation caused a decreased affinity and the range of this reduction varied widely from 1.4-fold over 700-fold. The affinity of the mutants correlated with the extent of impaired nuclear localization, and more importantly, with the duration of disease progression in ALS patients. This study provides a comprehensive understanding of the nuclear targeting mechanism of FUS and illustrates the significance of FUS-NLS in ALS.", "link"=>"http://www.mendeley.com/research/fusnlstransportin-1-complex-structure-provides-insights-nuclear-targeting-mechanism-fus-implications", "reader_count"=>52, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Student > Doctoral Student"=>4, "Researcher"=>13, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>1, "Other"=>1, "Student > Master"=>8, "Student > Bachelor"=>9, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Student > Doctoral Student"=>4, "Researcher"=>13, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>1, "Other"=>1, "Student > Master"=>8, "Student > Bachelor"=>9, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>15, "Agricultural and Biological Sciences"=>28, "Medicine and Dentistry"=>5, "Neuroscience"=>2, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>5}, "Neuroscience"=>{"Neuroscience"=>2}, "Chemistry"=>{"Chemistry"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>28}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>15}}, "reader_count_by_country"=>{"Canada"=>1, "United Kingdom"=>1, "Spain"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/298765", "https://ndownloader.figshare.com/files/298779", "https://ndownloader.figshare.com/files/298795", "https://ndownloader.figshare.com/files/298811", "https://ndownloader.figshare.com/files/298832", "https://ndownloader.figshare.com/files/298843", "https://ndownloader.figshare.com/files/298856"], "description"=>"<div><p>The C-terminal nuclear localization sequence of <u>FU</u>sed in <u>S</u>arcoma (FUS-NLS) is critical for its nuclear import mediated by transportin (Trn1). Familial amyotrophic lateral sclerosis (ALS) related mutations are clustered in FUS-NLS. We report here the structural, biochemical and cell biological characterization of the FUS-NLS and its clinical implications. The crystal structure of the FUS-NLS/Trn1 complex shows extensive contacts between the two proteins and a unique α-helical structure in the FUS-NLS. The binding affinity between Trn1 and FUS-NLS (wide-type and 12 ALS-associated mutants) was determined. As compared to the wide-type FUS-NLS (K<sub>D</sub> = 1.7 nM), each ALS-associated mutation caused a decreased affinity and the range of this reduction varied widely from 1.4-fold over 700-fold. The affinity of the mutants correlated with the extent of impaired nuclear localization, and more importantly, with the duration of disease progression in ALS patients. This study provides a comprehensive understanding of the nuclear targeting mechanism of FUS and illustrates the significance of FUS-NLS in ALS.</p> </div>", "links"=>[], "tags"=>["provides", "insights", "targeting", "fus", "implications", "als"], "article_id"=>118912, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0047056.s001", "https://dx.doi.org/10.1371/journal.pone.0047056.s002", "https://dx.doi.org/10.1371/journal.pone.0047056.s003", "https://dx.doi.org/10.1371/journal.pone.0047056.s004", "https://dx.doi.org/10.1371/journal.pone.0047056.s005", "https://dx.doi.org/10.1371/journal.pone.0047056.s006", "https://dx.doi.org/10.1371/journal.pone.0047056.s007"], "stats"=>{"downloads"=>36, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/FUS_NLS_Transportin_1_Complex_Structure_Provides_Insights_into_the_Nuclear_Targeting_Mechanism_of_FUS_and_the_Implications_in_ALS/118912", "title"=>"FUS-NLS/Transportin 1 Complex Structure Provides Insights into the Nuclear Targeting Mechanism of FUS and the Implications in ALS", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-10-08 02:28:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/562742"], "description"=>"<p>(A) Summary of the polar/electrostatic interactions between FUS-NLS (yellow) and Trn1 (cyan). FUS-NLS is divided into region I (E523–Y526), region II (D512–R522), and region III (P508–M511). (B) Schematic illustration of the hydrophobic contacts between the region I of FUS-NLS (E523–R524–P525–Y526) and Trn1. (C) Schematic illustration of the hydrophobic contacts between the region III of FUS-NLS (P508–G509–K510–M511) and Trn1. (D). The interaction between R524 and Q519, D520 and R522 within FUS-NLS. The figure is prepared with LIGPLOT <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047056#pone.0047056-Wallace1\" target=\"_blank\">[38]</a>.</p>", "links"=>[], "tags"=>["interactions", "trn1"], "article_id"=>233231, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0047056.g003", "stats"=>{"downloads"=>3, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_interactions_between_the_Trn1_and_the_FUS_NLS_/233231", "title"=>"The interactions between the Trn1 and the FUS-NLS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-08 00:53:51"}
  • {"files"=>["https://ndownloader.figshare.com/files/562646"], "description"=>"<p>(A) The overall structure. (B) The 2<i>F<sub>o</sub></i> − <i>F<sub>c</sub></i> composite omit electron density map around the FUS-NLS fragment (residues 508–526) contoured at 1.0 σ (gray mesh). The Trn1 and the FUS-NLS are shown in cyan and yellow, respectively. (C) The superimposition of residues 508–526 of FUS-NLS (yellow; PDB code: 4FQ3) with the corresponding regions from hnRNP A1-NLS (blue; PDB code: 2H4M), hnRNP D-NLS (grey; PDB code: 2Z5N), hnRNP M-NLS (magenta; PDB code: 2OT8), and TAP-NLS (cyan; PDB code: 2Z5K). The α-helix is unique in FUS-NLS whereas no specific secondary structure was found in the other structures.</p>", "links"=>[], "tags"=>["Computational biology", "biophysics", "neurological disorders", "Biochemistry"], "article_id"=>233136, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0047056.g002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_structure_of_the_FUS_NLS_Trn1_complex_/233136", "title"=>"The structure of the FUS-NLS/Trn1 complex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-08 00:52:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/562883"], "description"=>"<p>GFP-tagged WT full-length human FUS or different ALS mutants (S513P, G515C, R521G, R522G and P525L) were transfected into N2a cells. The cells were fixed in 4% paraformaldehyde and permeabilized by 0.1% Triton X-100 24 hours after transfection. The nuclei were stained by 4′,6-diamidino-2-phenylindole (DAPI). The coverslips were mounted and images were acquired using an Olympus confocal microscope (Olympus Fluoview, Ver.1.7c).</p>", "links"=>[], "tags"=>["localization", "wt", "mutant"], "article_id"=>233373, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0047056.g004", "stats"=>{"downloads"=>2, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Subcellular_localization_of_WT_and_mutant_FUS_/233373", "title"=>"Subcellular localization of WT and mutant FUS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-08 00:56:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/563110"], "description"=>"<p>The 12 ALS mutations are organized in the order of decreasing affinity.</p>a<p>The relative affinity is defined as <i>K</i><sub>D</sub> of WT (M) divided by <i>K</i><sub>D</sub> of the FUS-NLS mutants <i>(</i>M<i>).</i></p><p>The correlation coefficient χ<sup>2</sup> value is a statistical measure of how closely the fitted curve fits the experimental data <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047056#pone.0047056-Imasaki1\" target=\"_blank\">[15]</a> (see Methods).</p>", "links"=>[], "tags"=>["dissociation", "equilibrium", "constants", "trn1", "wild-type", "mutant"], "article_id"=>233593, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0047056.t001", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Association_rate_dissociation_rate_and_equilibrium_dissociation_constants_of_Trn1_and_wild_type_and_mutant_FUS_NLS_/233593", "title"=>"Association rate, dissociation rate, and equilibrium dissociation constants of Trn1 and wild-type and mutant FUS-NLS.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-10-08 00:59:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/563014"], "description"=>"<p>The coefficient of determination R<sup>2</sup> is 0.88, suggesting strong correlation. The number of patients for the R518K, R521G, R524S and P525L mutations are 12, 4, 2, and 8, respectively.</p>", "links"=>[], "tags"=>["duration", "familial", "als", "patients", "carrying", "r524s", "p525l", "mutations", "binding", "affinity", "mutant", "proteins"], "article_id"=>233491, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0047056.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Correlation_between_the_disease_duration_of_familial_ALS_patients_carrying_R518K_R521G_R524S_and_P525L_mutations_and_the_relative_binding_affinity_of_the_mutant_proteins_to_Trn1_/233491", "title"=>"Correlation between the disease duration of familial ALS patients carrying R518K, R521G, R524S and P525L mutations and the relative binding affinity of the mutant proteins to Trn1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-08 00:58:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/562555"], "description"=>"<p>(A). Domain structure of FUS with the C-terminal NLS. The ALS mutations are clustered in the NLS and the mutations studied here are shown in red. (B) Amino acid sequence alignments of FUS-NLS with other PY NLS’s from hnRNP A1, hnRNP D, hnRNP M and TAP. (C). Sequence alignment of FUS-NLS from different organisms.</p>", "links"=>[], "tags"=>["Computational biology", "biophysics", "neurological disorders", "Biochemistry"], "article_id"=>233042, "categories"=>["Biological Sciences", "Biochemistry", "Biophysics", "Neuroscience"], "users"=>["Chunyan Niu", "Jiayu Zhang", "Feng Gao", "Liuqing Yang", "Minze Jia", "Haining Zhu", "Weimin Gong"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0047056.g001", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequence_analysis_of_FUS_NLS_/233042", "title"=>"Sequence analysis of FUS-NLS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-08 00:50:42"}

PMC Usage Stats | Further Information

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Relative Metric

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