Histone Deacetylase 3 Promotes RCAN1 Stability and Nuclear Translocation
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{"title"=>"Histone deacetylase 3 promotes RCAN1 stability and nuclear translocation", "type"=>"journal", "authors"=>[{"first_name"=>"Kyung Ah", "last_name"=>"Han", "scopus_author_id"=>"57188946858"}, {"first_name"=>"Hye Seon", "last_name"=>"Kang", "scopus_author_id"=>"55261578900"}, {"first_name"=>"Jee Won", "last_name"=>"Lee", "scopus_author_id"=>"56804211000"}, {"first_name"=>"Lang", "last_name"=>"Yoo", "scopus_author_id"=>"25648678600"}, {"first_name"=>"Eunju", "last_name"=>"Im", "scopus_author_id"=>"36550386500"}, {"first_name"=>"Ahyoung", "last_name"=>"Hong", "scopus_author_id"=>"56572268300"}, {"first_name"=>"Yun Ju", "last_name"=>"Lee", "scopus_author_id"=>"56804039600"}, {"first_name"=>"Woo Hyun", "last_name"=>"Shin", "scopus_author_id"=>"57188953887"}, {"first_name"=>"Kwang Chul", "last_name"=>"Chung", "scopus_author_id"=>"35728207100"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "doi"=>"10.1371/journal.pone.0105416", "pui"=>"373801922", "sgr"=>"84928118048", "pmid"=>"25144594", "scopus"=>"2-s2.0-84928118048"}, "id"=>"fac11f8b-a080-3ef1-a64c-5ccebcbca154", "abstract"=>"Regulator of calcineurin 1 (RCAN1; also referred as DSCR1 or MCIP1) is located in close proximity to a Down syndrome critical region of human chromosome 21. Although RCAN1 is an endogenous inhibitor of calcineurin signaling that controls lymphocyte activation, apoptosis, heart development, skeletal muscle differentiation, and cardiac function, it is not yet clear whether RCAN1 might be involved in other cellular activities. In this study, we explored the extra-functional roles of RCAN1 by searching for novel RCAN1-binding partners. Using a yeast two-hybrid assay, we found that RCAN1 (RCAN1-1S) interacts with histone deacetylase 3 (HDAC3) in mammalian cells. We also demonstrate that HDAC3 deacetylates RCAN1. In addition, HDAC3 increases RCAN1 protein stability by inhibiting its poly-ubiquitination. Furthermore, HDAC3 promotes RCAN1 nuclear translocation. These data suggest that HDAC3, a new binding regulator of RCAN1, affects the protein stability and intracellular localization of RCAN1.", "link"=>"http://www.mendeley.com/research/histone-deacetylase-3-promotes-rcan1-stability-nuclear-translocation", "reader_count"=>7, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>2, "Student > Ph. D. Student"=>2, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>2, "Student > Ph. D. Student"=>2, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Agricultural and Biological Sciences"=>3, "Medicine and Dentistry"=>2, "Arts and Humanities"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>3}, "Unspecified"=>{"Unspecified"=>1}, "Arts and Humanities"=>{"Arts and Humanities"=>1}}, "reader_count_by_country"=>{"Israel"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1645220"], "description"=>"<p>Where indicated, HEK293 cells were transfected for 24 hr with Flag-HDAC3 alone or together with HA-tagged wild-type RCAN1, RCAN11-95, RCAN11-125, RCAN130-197 or RCAN196-197 fragments. Cells were lysed in the lysis buffer containing 8 M urea, and immunoblot analyses were performed using HA and Flag antibodies. The HSP90 antibody was used as a loading control.</p>", "links"=>[], "tags"=>["HDAC 3 increases RCAN 1 protein stability", "controls lymphocyte activation", "DSCR", "RCAN 1", "HDAC 3 deacetylates RCAN 1.", "MCIP", "Nuclear Translocation Regulator", "Histone Deacetylase 3 Promotes RCAN 1 Stability", "histone deacetylase 3"], "article_id"=>1147565, "categories"=>["Biological Sciences"], "users"=>["Kyung Ah Han", "Hye Seon Kang", "Jee Won Lee", "Lang Yoo", "Eunju Im", "Ahyoung Hong", "Yun Ju Lee", "Woo Hyun Shin", "Kwang Chul Chung"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0105416.g005", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_stabilizing_effect_of_HDAC3_is_dependent_on_the_RCAN1_N_terminal_30_8211_95th_amino_acid_/1147565", "title"=>"The stabilizing effect of HDAC3 is dependent on the RCAN1 N-terminal 30–95th amino acid.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-08-21 02:52:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/1645219"], "description"=>"<p>(<b>A</b>) HEK293 cells were transfected for 24 hr with HA-tagged RCAN1 alone or in combination with increasing amounts of Flag-HDAC3. RCAN1 and HDAC3 levels were examined by immunoblotting with anti-HA and anti-Flag antibodies. The HSP90 antibody was used as a loading control. (<b>B</b>) HEK293 cells were mock-transfected or transfected with Flag-HDAC3 for 24 hr. Whole cell lysates were subjected to western blot analysis with anti-RCAN1, anti-Flag, and anti-HSP90 antibodies (*, nonspecific bands). (<b>C</b>) HEK293 cells were transfected for 24 hr with HA-RCAN1 and/or Flag-HDAC3 and cell extracts were lysed with Triton X-100 (soluble) and SDS (insoluble)-containing buffer. Each fraction was analyzed by immunoblotting with anti-HA or anti-Flag antibodies. To demonstrate equal loading, cell lysates were analyzed with anti-Hsp90 antibody, as indicated. (<b>D, E</b>) Where indicated, HEK293 cells were transfected for 24 hr with HA-RCAN1 or Flag-HDAC3 alone or in combination. Cells were treated with 100 µM cycloheximide (CHX) for the indicated times and harvested in PBS. RCAN1 levels in each sample were determined by western blot analyses using anti-HA antibodies (<b>D</b>). Data are representative of three independent experiments. Relative RCAN1 protein levels were quantified using the Multi Gauge V 3.1 program (*, <i>p</i><0.05; **, <i>p</i><0.01; ***, <i>p</i><0.001; <b>E</b>). (<b>F, G</b>) HEK293 cells were transfected for 24 hr with HA-RCAN1 or Flag-HDAC3 alone or in combination and treated for 6 hr with 10 µM MG132, as indicated. Cell lysates were immunoprecipitated using anti-HA antibody and immunoblotted using anti-ubiquitin or anti-HA antibodies. Proper expression of ubiquitin, RCAN1, or HDAC3 in cell extracts was determined by immunoblotting with their antibodies (<b>F</b>). Data are representative of three independent experiments. Relative ubiquitinated RCAN1 protein levels were quantified using the Multi Gauge V 3.1 program (*, <i>p</i><0.05; <b>G</b>).</p>", "links"=>[], "tags"=>["HDAC 3 increases RCAN 1 protein stability", "controls lymphocyte activation", "DSCR", "RCAN 1", "HDAC 3 deacetylates RCAN 1.", "MCIP", "Nuclear Translocation Regulator", "Histone Deacetylase 3 Promotes RCAN 1 Stability", "histone deacetylase 3"], "article_id"=>1147564, "categories"=>["Biological Sciences"], "users"=>["Kyung Ah Han", "Hye Seon Kang", "Jee Won Lee", "Lang Yoo", "Eunju Im", "Ahyoung Hong", "Yun Ju Lee", "Woo Hyun Shin", "Kwang Chul Chung"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0105416.g004", "stats"=>{"downloads"=>4, "page_views"=>77, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HDAC3_overexpression_increases_RCAN1_stability_by_inhibiting_RCAN1_ubiquitination_/1147564", "title"=>"HDAC3 overexpression increases RCAN1 stability by inhibiting RCAN1 ubiquitination.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-08-21 02:52:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/1645216"], "description"=>"<p>(<b>A</b>) Where indicated, HEK293 cells were mock-transfected or transfected with plasmids encoding HA-tagged RCAN1 and/or Flag-tagged HDAC3 for 24 hr. Cell lysates were immunoprecipitated using anti-HA and anti-Flag antibodies, and immunocomplexes were analyzed by Western blotting using anti-HA or anti-Flag antibodies. Expression of transiently transfected proteins in cell lysates was identified using immunoblot analyses, as indicated. (<b>B, C</b>) HEK293 cell lysates were immunoprecipitated with anti-RCAN1 (<b>B</b>), anti-HDAC3 antibodies (<b>C</b>), or normal rabbit IgGs followed by immunoblotting using anti-HDAC3 and anti-RCAN1 antibodies, as indicated (*, nonspecific bands).</p>", "links"=>[], "tags"=>["HDAC 3 increases RCAN 1 protein stability", "controls lymphocyte activation", "DSCR", "RCAN 1", "HDAC 3 deacetylates RCAN 1.", "MCIP", "Nuclear Translocation Regulator", "Histone Deacetylase 3 Promotes RCAN 1 Stability", "histone deacetylase 3"], "article_id"=>1147561, "categories"=>["Biological Sciences"], "users"=>["Kyung Ah Han", "Hye Seon Kang", "Jee Won Lee", "Lang Yoo", "Eunju Im", "Ahyoung Hong", "Yun Ju Lee", "Woo Hyun Shin", "Kwang Chul Chung"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0105416.g001", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_RCAN1_binds_HDAC3_in_HEK293_cells_/1147561", "title"=>"RCAN1 binds HDAC3 in HEK293 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-08-21 02:52:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/1645221"], "description"=>"<p>(<b>A, B</b>) HEK293 cells were transfected for 24 hr with HA-RCAN1 and/or Flag-HDAC3 and fractionated into cytosolic and nuclear fractions. The fractions were analyzed by immunoblot using anti-HA or anti-Flag antibodies. The purity of each fraction was confirmed by immunoblotting with α-tubulin (cytosolic marker) or histone H1 (nuclear marker) (<b>A</b>). Data are representative of three independent experiments. Relative cytosolic RCAN1 and nuclear RCAN1 protein levels were quantified using the Multi Gauge V 3.1 program (**, <i>p</i><0.01; <b>B</b>). (<b>C</b>) HEK293 cells were transfected for 24 hr with HA-RCAN1 or/and Flag-HDAC3, fixed and permeabilized, and labeled with anti-HA or Flag antibodies. The cells were then stained with Alexa Fluor 488-conjugated anti-mouse and Alexa Fluor 594-conjugated anti-rabbit secondary antibodies. Nuclei were counterstained with DAPI, and immunostained preparations were visualized by confocal microscopy. Scale bars: 10 µm (<b>D</b>) HEK293 cell were transfected for 24 hr with HA-RCAN1 and/or Flag-HDAC3, and fractionated into the cytosolic and nuclear fractions. These fractions were immunoprecipitated with anti-acetyl-Lys antibodies, followed by immunoblotting with anti-HA antiserum. The expression of exogenously added RCAN1 or HDAC3 protein in each fraction was analyzed by immunoblotting anti-HA or Flag antibodies. The purity of each fraction was confirmed by immunoblotting with α-tubulin (cytosolic marker) or histone H3 (nuclear marker).</p>", "links"=>[], "tags"=>["HDAC 3 increases RCAN 1 protein stability", "controls lymphocyte activation", "DSCR", "RCAN 1", "HDAC 3 deacetylates RCAN 1.", "MCIP", "Nuclear Translocation Regulator", "Histone Deacetylase 3 Promotes RCAN 1 Stability", "histone deacetylase 3"], "article_id"=>1147566, "categories"=>["Biological Sciences"], "users"=>["Kyung Ah Han", "Hye Seon Kang", "Jee Won Lee", "Lang Yoo", "Eunju Im", "Ahyoung Hong", "Yun Ju Lee", "Woo Hyun Shin", "Kwang Chul Chung"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0105416.g006", "stats"=>{"downloads"=>0, "page_views"=>63, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HDAC3_induces_nuclear_translocation_of_cytosolic_RCAN1_/1147566", "title"=>"HDAC3 induces nuclear translocation of cytosolic RCAN1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-08-21 02:52:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/1645218"], "description"=>"<p>Where indicated, HEK293 cells were transfected for 24 hr with HA-RCAN1 and/or Flag-HDAC3 (H3), and treated for 3 hr with 3 µM trichostatin A (TSA). Cell lysates were immunoprecipitated with anti-acetyl-Lys antibodies, followed by immunoblotting with anti-HA antiserum. Total lysates were analyzed by immunoblot using anti-HA or Flag antibodies. The HSP90 antibody was used as a loading control.</p>", "links"=>[], "tags"=>["HDAC 3 increases RCAN 1 protein stability", "controls lymphocyte activation", "DSCR", "RCAN 1", "HDAC 3 deacetylates RCAN 1.", "MCIP", "Nuclear Translocation Regulator", "Histone Deacetylase 3 Promotes RCAN 1 Stability", "histone deacetylase 3"], "article_id"=>1147563, "categories"=>["Biological Sciences"], "users"=>["Kyung Ah Han", "Hye Seon Kang", "Jee Won Lee", "Lang Yoo", "Eunju Im", "Ahyoung Hong", "Yun Ju Lee", "Woo Hyun Shin", "Kwang Chul Chung"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0105416.g003", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_HDAC3_targets_to_and_deacetylates_RCAN1_/1147563", "title"=>"HDAC3 targets to and deacetylates RCAN1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-08-21 02:52:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/1645217"], "description"=>"<p>(<b>A</b>) Diagram of HA-tagged wild-type RCAN1 and its deletion mutants. RCAN1 consists of an N-terminal amphipathic leucine repeat (L) domain, a central span of 31 amino acids containing a serine-proline (SP) repeat, a C-terminal acidic region (a), and a cluster of basic amino acids (b). AS denotes the alternative splicing site of <i>RCAN1</i> between exon 1 or 4 and exon 5. (<b>B</b>) HEK293 cells were transfected for 24 hr with Flag-HDAC3 alone or in combination with various HA-tagged deletion RCAN1 mutants and treated for 6 hr with 10 µM MG132, as indicated. Total lysates and anti-Flag immunoprecipitates were analyzed by immunoblot using anti-HA or anti-Flag antibodies.</p>", "links"=>[], "tags"=>["HDAC 3 increases RCAN 1 protein stability", "controls lymphocyte activation", "DSCR", "RCAN 1", "HDAC 3 deacetylates RCAN 1.", "MCIP", "Nuclear Translocation Regulator", "Histone Deacetylase 3 Promotes RCAN 1 Stability", "histone deacetylase 3"], "article_id"=>1147562, "categories"=>["Biological Sciences"], "users"=>["Kyung Ah Han", "Hye Seon Kang", "Jee Won Lee", "Lang Yoo", "Eunju Im", "Ahyoung Hong", "Yun Ju Lee", "Woo Hyun Shin", "Kwang Chul Chung"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0105416.g002", "stats"=>{"downloads"=>1, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_N_terminal_30_95_th_amino_acid_region_of_RCAN1_is_critical_for_HDAC3_binding_/1147562", "title"=>"The N-terminal 30–95<sup>th</sup> amino acid region of RCAN1 is critical for HDAC3 binding.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-08-21 02:52:27"}

PMC Usage Stats | Further Information

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Relative Metric

{"start_date"=>"2014-01-01T00:00:00Z", "end_date"=>"2014-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[291]}, {"subject_area"=>"/Biology and life sciences/Cell biology", "average_usage"=>[286]}, {"subject_area"=>"/Biology and life sciences/Genetics", "average_usage"=>[306, 482]}]}
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