BIG3 Inhibits the Estrogen-Dependent Nuclear Translocation of PHB2 via Multiple Karyopherin-Alpha Proteins in Breast Cancer Cells
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{"title"=>"BIG3 Inhibits the estrogen-dependent nuclear translocation of PHB2 via multiple karyopherin-alpha proteins in breast cancer cells", "type"=>"journal", "authors"=>[{"first_name"=>"Nam Hee", "last_name"=>"Kim", "scopus_author_id"=>"56076337800"}, {"first_name"=>"Tetsuro", "last_name"=>"Yoshimaru", "scopus_author_id"=>"6603373014"}, {"first_name"=>"Yi An", "last_name"=>"Chen", "scopus_author_id"=>"55895369000"}, {"first_name"=>"Taisuke", "last_name"=>"Matsuo", "scopus_author_id"=>"22951088000"}, {"first_name"=>"Masato", "last_name"=>"Komatsu", "scopus_author_id"=>"34972855200"}, {"first_name"=>"Yasuo", "last_name"=>"Miyoshi", "scopus_author_id"=>"56844688000"}, {"first_name"=>"Eiji", "last_name"=>"Tanaka", "scopus_author_id"=>"35351574300"}, {"first_name"=>"Mitsunori", "last_name"=>"Sasa", "scopus_author_id"=>"7101930078"}, {"first_name"=>"Kenji", "last_name"=>"Mizuguchi", "scopus_author_id"=>"7101693768"}, {"first_name"=>"Toyomasa", "last_name"=>"Katagiri", "scopus_author_id"=>"7201387569"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"84936761474", "scopus"=>"2-s2.0-84936761474", "pui"=>"605098240", "pmid"=>"26052702", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0127707"}, "id"=>"b84f35aa-9bb9-3866-882b-ebeedb437a32", "abstract"=>"We recently reported that brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) binds Prohibitin 2 (PHB2) in cytoplasm, thereby causing a loss of function of the PHB2 tumor suppressor in the nuclei of breast cancer cells. However, little is known regarding the mechanism by which BIG3 inhibits the nuclear translocation of PHB2 into breast cancer cells. Here, we report that BIG3 blocks the estrogen (E2)-dependent nuclear import of PHB2 via the karyopherin alpha (KPNA) family in breast cancer cells. We found that overexpressed PHB2 interacted with KPNA1, KPNA5, and KPNA6, thereby leading to the E2-dependent translocation of PHB2 into the nuclei of breast cancer cells. More importantly, knockdown of each endogenous KPNA by siRNA caused a significant inhibition of E2-dependent translocation of PHB2 in BIG3-depleted breast cancer cells, thereby enhancing activation of estrogen receptor alpha (ERα). These data indicated that BIG3 may block the KPNAs (KPNA1, KPNA5, and KPNA6) binding region(s) of PHB2, thereby leading to inhibition of KPNAs-mediated PHB2 nuclear translocation in the presence of E2 in breast cancer cells. Understanding this regulation of PHB2 nuclear import may provide therapeutic strategies for controlling E2/ERα signals in breast cancer cells.", "link"=>"http://www.mendeley.com/research/big3-inhibits-estrogendependent-nuclear-translocation-phb2-via-multiple-karyopherinalpha-proteins-br", "reader_count"=>11, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>2, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>1, "Student > Master"=>3, "Student > Bachelor"=>2, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>2, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>1, "Student > Master"=>3, "Student > Bachelor"=>2, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>3, "Medicine and Dentistry"=>2, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>3}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/2100543", "https://ndownloader.figshare.com/files/2100544", "https://ndownloader.figshare.com/files/2100545", "https://ndownloader.figshare.com/files/2100546", "https://ndownloader.figshare.com/files/2100547", "https://ndownloader.figshare.com/files/2100548", "https://ndownloader.figshare.com/files/2100549"], "description"=>"<div><p>We recently reported that brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) binds Prohibitin 2 (PHB2) in cytoplasm, thereby causing a loss of function of the PHB2 tumor suppressor in the nuclei of breast cancer cells. However, little is known regarding the mechanism by which BIG3 inhibits the nuclear translocation of PHB2 into breast cancer cells. Here, we report that BIG3 blocks the estrogen (E2)-dependent nuclear import of PHB2 via the karyopherin alpha (KPNA) family in breast cancer cells. We found that overexpressed PHB2 interacted with KPNA1, KPNA5, and KPNA6, thereby leading to the E2-dependent translocation of PHB2 into the nuclei of breast cancer cells. More importantly, knockdown of each endogenous KPNA by siRNA caused a significant inhibition of E2-dependent translocation of PHB2 in BIG3-depleted breast cancer cells, thereby enhancing activation of estrogen receptor alpha (ERα). These data indicated that BIG3 may block the KPNAs (KPNA1, KPNA5, and KPNA6) binding region(s) of PHB2, thereby leading to inhibition of KPNAs-mediated PHB2 nuclear translocation in the presence of E2 in breast cancer cells. Understanding this regulation of PHB2 nuclear import may provide therapeutic strategies for controlling E2/ERα signals in breast cancer cells.</p></div>", "links"=>[], "tags"=>["PHB 2", "BIG 3 Inhibits", "er", "breast cancer cells", "BIG 3 blocks", "overexpressed PHB 2 interacted", "kpna", "BIG 3", "translocation", "PHB 2 tumor suppressor"], "article_id"=>1440641, "categories"=>["Biological Sciences"], "users"=>["Nam-Hee Kim", "Tetsuro Yoshimaru", "Yi-An Chen", "Taisuke Matsuo", "Masato Komatsu", "Yasuo Miyoshi", "Eiji Tanaka", "Mitsunori Sasa", "Kenji Mizuguchi", "Toyomasa Katagiri"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0127707.s001", "https://dx.doi.org/10.1371/journal.pone.0127707.s002", "https://dx.doi.org/10.1371/journal.pone.0127707.s003", "https://dx.doi.org/10.1371/journal.pone.0127707.s004", "https://dx.doi.org/10.1371/journal.pone.0127707.s005", "https://dx.doi.org/10.1371/journal.pone.0127707.s006", "https://dx.doi.org/10.1371/journal.pone.0127707.s007"], "stats"=>{"downloads"=>6, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_BIG3_Inhibits_the_Estrogen_Dependent_Nuclear_Translocation_of_PHB2_via_Multiple_Karyopherin_Alpha_Proteins_in_Breast_Cancer_Cells_/1440641", "title"=>"BIG3 Inhibits the Estrogen-Dependent Nuclear Translocation of PHB2 via Multiple Karyopherin-Alpha Proteins in Breast Cancer Cells", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2015-06-08 03:46:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/2100530"], "description"=>"<p>(A) The expression levels of the KPNA family of proteins in breast cancer cell lines and normal human mammary gland tissue were evaluated using semi-quantitative RT-PCR. <i>ACTB</i> is used as an internal control; (B, C) Immunoblotting analysis was performed to assess the interactions between PHB2 (B) or PHB2 NLS mutants (C) and each KPNA. The lysates from COS-7 cells transfected with PHB2 or PHB2 NLS mutants and each KPNA were immunoprecipitated with anti-FLAG antibody. Full-length images of immunoblots and semi-quantitative RT-PCR are shown in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0127707#pone.0127707.s001\" target=\"_blank\">S1A–S1C Fig</a> The data are expressed the fold increase over HA-PHB2 which bound to KPNA1 (set at 1.0) (B).</p>", "links"=>[], "tags"=>["PHB 2", "BIG 3 Inhibits", "er", "breast cancer cells", "BIG 3 blocks", "overexpressed PHB 2 interacted", "kpna", "BIG 3", "translocation", "PHB 2 tumor suppressor"], "article_id"=>1440632, "categories"=>["Biological Sciences"], "users"=>["Nam-Hee Kim", "Tetsuro Yoshimaru", "Yi-An Chen", "Taisuke Matsuo", "Masato Komatsu", "Yasuo Miyoshi", "Eiji Tanaka", "Mitsunori Sasa", "Kenji Mizuguchi", "Toyomasa Katagiri"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0127707.g001", "stats"=>{"downloads"=>2, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PHB2_interact_with_KPNAs_/1440632", "title"=>"PHB2 interact with KPNAs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-08 03:46:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/2100536"], "description"=>"<p>(A) Immunoblotting analysis was performed to detect the subcellular localization of KPNA, ERα and PHB2. COS-7 cells co-transfected with HA-PHB2, each FLAG-KPNA and FLAG-ERα were treated with 10 nM E2 for 24 h and separated into cytoplasmic and nuclear fractions. Each KPNAs and ERα were detected by endogenous antibody. α/β-Tubulin (tubulin) and lamin B1 (lamin) were used as loading controls for the cytoplasmic (Cyto) and nuclear (N) fractions, respectively. (B) Representative immunofluorescence images of the subcellular localization of HA-PHB2 in COS-7 cells are shown; HA-PHB2 (red), DAPI (blue). (C) Statistical analyses of the nuclear intensity of translocated PHB2. The data represent the mean ± SD of four different points (***<i>P</i><0.001 in a two-sided Student’s <i>t</i>-test).</p>", "links"=>[], "tags"=>["PHB 2", "BIG 3 Inhibits", "er", "breast cancer cells", "BIG 3 blocks", "overexpressed PHB 2 interacted", "kpna", "BIG 3", "translocation", "PHB 2 tumor suppressor"], "article_id"=>1440634, "categories"=>["Biological Sciences"], "users"=>["Nam-Hee Kim", "Tetsuro Yoshimaru", "Yi-An Chen", "Taisuke Matsuo", "Masato Komatsu", "Yasuo Miyoshi", "Eiji Tanaka", "Mitsunori Sasa", "Kenji Mizuguchi", "Toyomasa Katagiri"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0127707.g002", "stats"=>{"downloads"=>0, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_KPNA_mediates_the_nuclear_translocation_of_PHB2_/1440634", "title"=>"KPNA mediates the nuclear translocation of PHB2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-08 03:46:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/2100537"], "description"=>"<p>(A) Immunoblotting analysis was performed to evaluate the subcellular localization of endogenous PHB2 in the BIG3- and KPNAs (KPNA1, KPNA5, and KPNA6)-depleted MCF-7 cells. MCF-7 cells were treated with siBIG3 and each siKPNA, followed by E2 ± ERAP for 24 h. Then, the cells were separated into cytoplasmic and nuclear fractions; (B) The nuclear translocation of PHB2 in KPNA-depleted MCF-7 cells in the presence of E2 and ERAP was evaluated. MCF-7 cells were treated with each siKPNA followed by E2 ± ERAP for 24 h. Then, the cells were separated into cytoplasmic (Cyto) and nuclear (N) fractions. The data are expressed the fold increase over cytoplasm fraction of untreated siEGFP, siKPNA1, siKPNA2, siKPNA5 or siKPNA6-transfected cells (set at 1.0), respectively. (C) The relationship among each KPNA was evaluated in KPNA-depleted MCF-7 cells in presence of E2 and ERAP. α/β-Tubulin (tubulin) and lamin B1 (lamin) were used as loading controls for the cytoplasmic (Cyto) and nuclear (N) fractions, respectively (A, B). Full-length images of immunoblots are shown in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0127707#pone.0127707.s003\" target=\"_blank\">S3A–S3C Fig</a>.</p>", "links"=>[], "tags"=>["PHB 2", "BIG 3 Inhibits", "er", "breast cancer cells", "BIG 3 blocks", "overexpressed PHB 2 interacted", "kpna", "BIG 3", "translocation", "PHB 2 tumor suppressor"], "article_id"=>1440635, "categories"=>["Biological Sciences"], "users"=>["Nam-Hee Kim", "Tetsuro Yoshimaru", "Yi-An Chen", "Taisuke Matsuo", "Masato Komatsu", "Yasuo Miyoshi", "Eiji Tanaka", "Mitsunori Sasa", "Kenji Mizuguchi", "Toyomasa Katagiri"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0127707.g003", "stats"=>{"downloads"=>4, "page_views"=>100, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_KPNA1_KPNA5_and_KPNA6_are_required_for_E2_dependent_PHB2_nuclear_import_in_breast_cancer_cells_/1440635", "title"=>"KPNA1, KPNA5, and KPNA6 are required for E2-dependent PHB2 nuclear import in breast cancer cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-08 03:46:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/2100539"], "description"=>"<p>(A) Immunoblotting analysis was performed to evaluate the interactions between ERα and PHB2 in BIG3- and KPNA (KPNA1, KPNA5, and KPNA6)-depleted MCF-7 cells. MCF-7 cells were treated with siBIG3 and each siKPNA, followed by E2 ± ERAP for 24 h. Then, the nuclear fractions were immunoprecipitated with anti-ERα antibody and were immunoblotted with antibodies against the indicated proteins. The data are expressed the fold increase over E2-treated siBIG3-transfected cells of right and left panels, respectively (set at 1.0). ND: not detected. This experiment was performed using the nuclear fractions used in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0127707#pone.0127707.g003\" target=\"_blank\">Fig 3A</a>; (B) The interaction between ERα and PHB2 released by E2 and ERAP in the nuclear fractions was evaluated. MCF-7 cells depleted of each KPNA were treated with E2 ± ERAP for 24 h, and the nuclear fractions were immunoprecipitated with anti-ERα antibody. The data are expressed the fold increase over E2-treated siEGFP-transfected cells of right and left panels, respectively (set at 1.0). This experiment was performed using the nuclear fractions used in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0127707#pone.0127707.g003\" target=\"_blank\">Fig 3B</a>; (C) The <i>TFF1</i> expression levels following treatment with siBIG3 and siKPNA were evaluated using real-time PCR. The data are expressed as the fold increase over the untreated cells (set at 1.0) and represent the means ± SD of two independent experiments (**<i>P</i><0.01, ***<i>P</i><0.001 in a two-sided Student’s <i>t</i>-test); (D) Immunoblotting analysis was performed to identify the KPNA-binding regions in PHB2. The lysates from COS-7 cells transfected with the indicated HA-PHB2 constructs and FLAG-KPNAs were immunoprecipitated with an anti-FLAG antibody; (E) Immunoblotting analysis was performed to identify the BIG3-binding region in PHB2. The lysates from HEK293T cells transfected with the indicated HA-PHB2 constructs and FLAG-BIG3 were immunoprecipitated with an anti-FLAG antibody. Full-length images of immunoblots are shown in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0127707#pone.0127707.s006\" target=\"_blank\">S6A–S6D Fig</a>.</p>", "links"=>[], "tags"=>["PHB 2", "BIG 3 Inhibits", "er", "breast cancer cells", "BIG 3 blocks", "overexpressed PHB 2 interacted", "kpna", "BIG 3", "translocation", "PHB 2 tumor suppressor"], "article_id"=>1440637, "categories"=>["Biological Sciences"], "users"=>["Nam-Hee Kim", "Tetsuro Yoshimaru", "Yi-An Chen", "Taisuke Matsuo", "Masato Komatsu", "Yasuo Miyoshi", "Eiji Tanaka", "Mitsunori Sasa", "Kenji Mizuguchi", "Toyomasa Katagiri"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0127707.g005", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_KPNA1_KPNA5_and_KPNA6_induce_E2_dependent_nuclear_translocation_of_PHB2_/1440637", "title"=>"KPNA1, KPNA5, and KPNA6 induce E2-dependent nuclear translocation of PHB2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-08 03:46:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/2100541"], "description"=>"<p>The mechanism of the E2-dependent nuclear translocation of PHB2 through KPNAs in breast cancer cells.</p>", "links"=>[], "tags"=>["PHB 2", "BIG 3 Inhibits", "er", "breast cancer cells", "BIG 3 blocks", "overexpressed PHB 2 interacted", "kpna", "BIG 3", "translocation", "PHB 2 tumor suppressor"], "article_id"=>1440639, "categories"=>["Biological Sciences"], "users"=>["Nam-Hee Kim", "Tetsuro Yoshimaru", "Yi-An Chen", "Taisuke Matsuo", "Masato Komatsu", "Yasuo Miyoshi", "Eiji Tanaka", "Mitsunori Sasa", "Kenji Mizuguchi", "Toyomasa Katagiri"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0127707.g006", "stats"=>{"downloads"=>7, "page_views"=>136, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_mechanism_of_the_E2_dependent_nuclear_translocation_of_PHB2_through_KPNAs_in_breast_cancer_cells_/1440639", "title"=>"The mechanism of the E2-dependent nuclear translocation of PHB2 through KPNAs in breast cancer cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-08 03:46:09"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"9", "full-text"=>"7", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"2"}
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  • {"unique-ip"=>"13", "full-text"=>"13", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"8", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
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  • {"unique-ip"=>"14", "full-text"=>"15", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"12", "full-text"=>"13", "pdf"=>"7", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"9", "full-text"=>"10", "pdf"=>"10", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"5"}
  • {"unique-ip"=>"11", "full-text"=>"10", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"6", "supp-data"=>"3", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"11", "full-text"=>"13", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"8", "full-text"=>"10", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"12", "full-text"=>"12", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"11", "full-text"=>"11", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"20", "full-text"=>"15", "pdf"=>"9", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"13", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"24", "full-text"=>"21", "pdf"=>"11", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}

Relative Metric

{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}
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