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{"title"=>"The ciliary protein cystin forms a regulatory complex with necdin to modulate myc expression", "type"=>"journal", "authors"=>[{"first_name"=>"Maoqing", "last_name"=>"Wu", "scopus_author_id"=>"55873458600"}, {"first_name"=>"Chaozhe", "last_name"=>"Yang", "scopus_author_id"=>"25640457200"}, {"first_name"=>"Binli", "last_name"=>"Tao", "scopus_author_id"=>"56249431300"}, {"first_name"=>"Su", "last_name"=>"Bu", "scopus_author_id"=>"15843185600"}, {"first_name"=>"Lisa M.", "last_name"=>"Guay-Woodford", "scopus_author_id"=>"7006429877"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"24349431", "pui"=>"372133158", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0083062", "scopus"=>"2-s2.0-84892623705", "sgr"=>"84892623705"}, "id"=>"ecc2a770-7242-3c19-b1f2-17b0f1d25c76", "abstract"=>"Cystin is a novel cilia-associated protein that is disrupted in the cpk mouse, a well-characterized mouse model of autosomal recessive polycystic kidney disease (ARPKD). Interestingly, overexpression of the Myc gene is evident in animal models of ARPKD and is thought to contribute to the renal cystic phenotype. Using a yeast two-hybrid approach, the growth suppressor protein necdin, known to modulate Myc expression, was found as an interacting partner of cystin. Deletion mapping demonstrated that the C-terminus of cystin and both termini of necdin are required for their mutual interaction. Speculating that these two proteins may function to regulate gene expression, we developed a luciferase reporter assay and observed that necdin strongly activated the Myc P1 promoter, and cystin did so more modestly. Interestingly, the necdin effect was significantly abrogated when cystin was co-transfected. Chromatin immunoprecipitation and electrophoretic mobility shift assays revealed a physical interaction with both necdin and cystin and the Myc P1 promoter, as well as between these proteins. The data suggest that these proteins likely function in a regulatory complex. Thus, we speculate that Myc overexpression in the cpk kidney results from the dysregulation of the cystin-necdin regulatory complex and c-Myc, in turn, contributes to cystogenesis in the cpk mouse.", "link"=>"http://www.mendeley.com/research/ciliary-protein-cystin-forms-regulatory-complex-necdin-modulate-myc-expression", "reader_count"=>10, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>1, "Student > Ph. D. Student"=>3, "Student > Postgraduate"=>2, "Other"=>1, "Lecturer"=>1, "Student > Doctoral Student"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>1, "Student > Ph. D. Student"=>3, "Student > Postgraduate"=>2, "Other"=>1, "Lecturer"=>1, "Student > Doctoral Student"=>1}, "reader_count_by_subject_area"=>{"Agricultural and Biological Sciences"=>5, "Medicine and Dentistry"=>5}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>5}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>5}}, "reader_count_by_country"=>{"United States"=>1, "Japan"=>1}, "group_count"=>0}

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• http://doi.org/10.1152/ajprenal.00489.2017
• http://doi.org/10.1152/ajprenal.00167.2016
• http://doi.org/10.1016/j.omtm.2019.03.001

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/1311590"], "description"=>"<p>(<b>A</b>) RT-PCR was performed to detect the expression of cystin and necdin in mIMCD-3 cells. Total RNA was isolated from confluent mIMCD-3 cells and equal amounts of cDNA were used as a template for RT-PCR. Primer pairs for cystin and necdin were designed to amplify 207 bp and 632 bp target bands, respectively. β-actin was used as a positive control; water was used as a negative control. The PCR products were excised from the gel, purified, and verified by sequencing (data not shown). (<b>B</b>) Western blot analysis of endogenous cystin in confluent mIMCD-3 cells. The cells were fractioned to cytoplasmic, membrane, and nuclear fractions. Analysis of control proteins for the different fractions were shown in the lower panel. Endogenous cystin migrates at 25 kDa and accumulated in the membrane fraction. <b>(C)</b> Western blot analysis of endogenous necdin in confluent mIMCD-3 cells. Endogenous necdin was detected in the nuclear fraction and migrated at 40 kD when probed with a necdin N-terminal antibody (N20, arrowhead). Western blot analysis of Myc-necdin in mIMCD-3 cells using a myc antibody also reveals a band at 40 kD (right). The band at ∼30 kDa is an unidentified artifact of the antibody used <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0083062#pone.0083062-DeCamilli1\" target=\"_blank\">[103]</a>.</p>", "links"=>[], "tags"=>["cystin", "necdin", "mimcd-3"], "article_id"=>875034, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g003", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Endogenous_cystin_and_necdin_were_expressed_in_mIMCD_3_cells_/875034", "title"=>"Endogenous cystin and necdin were expressed in mIMCD-3 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311603"], "description"=>"<p>+LgT and Lam+LgT were used as positive and negative controls, respectively for protein interaction. Necdin was identified from a cDNA library as a full-length cystin binding partner. LgT: large T-antigen; Lam: human lamin C. pGBKT7 is a bait vector containing the GAL4 DNA binding domain; pGADT7 and pACT2 are prey vectors containing the GAL4 activation domain. p53</p>", "links"=>[], "tags"=>["validation", "necdin", "cystin"], "article_id"=>875047, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.t001", "stats"=>{"downloads"=>2, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Y2H_validation_of_the_necdin_and_cystin_interaction_/875047", "title"=>"Y2H validation of the necdin and cystin interaction.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311599"], "description"=>"<p>(<b>A</b>) Schematic representation of the <i>Myc</i> P1 promoter (–88 ∼ +47) fragment in the pGL4.22 luciferase vector used for chromatin immunoprecipitation (ChIP). The ChIP primers (F and R) spanned the promoter region. The right panel showes the 23-bp EMSA probe, containing the <i>Myc</i> P1 GN-box (underlined). (<b>B</b>) ChIP was performed to identify the interaction of necdin, cystin, and cystin-C25 with the <i>Myc</i> P1 promoter fragment. After sonication, the protein-DNA complexes were immunoprecipitated either with the anti-necdin (N143) or cystin (70053) antibody. <b>(C)</b> Western blot analysis confirmed that each of the constructs were highly expressed in the ChIP experiments. HA-cystin/HA-cystin-C25 were detected with the anti-cystin antibodies (70053) and myc-necdin was detected with an anti-necdin antibody (N143). (<b>D</b>) EMSA was performed to analyze the binding of necdin and cystin to the <i>Myc</i> P1 DNA fragment. The biotin-labeled probe (A right panel) containing the <i>Myc</i> P1 GN box was incubated with nuclear extracts from mIMCD-3 cells transfected with wild-type cystin and necdin. Both cystin and necdin bound to the <i>Myc</i> P1 GN box (lanes 3, 5) and this binding was efficiently abolished by unlabeled probe. (<b>E</b>) Immunoblotting analysis of the EMSA samples indicated robust expression of HA-cystin and myc-necdin in nuclear extracts, histone H3 was used as a loading control.</p>", "links"=>[], "tags"=>["necdin", "cystin", "p1", "promoter"], "article_id"=>875043, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g007", "stats"=>{"downloads"=>2, "page_views"=>41, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Both_necdin_and_cystin_bind_to_Myc_P1_promoter_DNA_/875043", "title"=>"Both necdin and cystin bind to <i>Myc</i> P1 promoter DNA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311592"], "description"=>"<p>The subcellular localization of cystin and its variants was determined by immunoblotting. The wild-type cystin_wt, the N-terminal deletion mutant cystin_▵1-20, and the site-directed mutant cystin_G2A, each tagged with GFP were stably-transfected in mIMCD-3 cells. (<b>A</b>) The distribution of wild-type cystin_wt::GFP in the four fractions prepared from mIMCD-3 cells is shown by western blot (above) and using densitometry (below). (<b>B</b>) The distribution for cystin_▵1-20::GFP is similarly shown by western and densitometry. (<b>C</b>) The distribution of the site-directed mutant cystin_G2A::GFP is shown in the four fractions of mIMCD-3 cells using western blot analysis and densitometry. (<b>D</b>) To demonstrate the reliability of the fractionation protocol, wild type mIMCD-3 cells were fractionated (n = 5 experiments) and 10 µg of each fraction was analyzed by western blotting with fraction specific marker as indicated. The fractions are cytosol (1), membrane (2), nuclear (3) and cytoskeleton (4).</p>", "links"=>[], "tags"=>["localization"], "article_id"=>875036, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g004", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cystin_has_a_functional_nuclear_localization_signal_at_the_N_terminus_/875036", "title"=>"Cystin has a functional nuclear localization signal at the N-terminus.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311588"], "description"=>"<p>(<b>A</b>) GST pull-down was used to verify the interaction between cystin and necdin. pCMV-GST-cystin and pCMV-myc-necdin were co-transfected into COS-7 cells. The precipitated samples were run on a PAGE gel and probed with myc (lanes 1-4) and GST antibodies (lanes 5-8). Whole cell lysate was used to assess protein expression (lane 1-2 and 5-6). Compared to the negative control (lane 3), the specific interaction between cystin and necdin is clear (lane 4, arrowhead). (<b>B</b>) Co-IP was used to verify the interaction between cystin and necdin. pCMV-HA-cystin and pCMV-myc-necdin were co-transfected into COS-7 cells. The protein complex of HA-cystin and myc-necdin in the cell lysate was precipitated using the HA tag, and the samples were probed with myc (lanes 1-4) and cystin antibodies (lanes 5-8), respectively. Whole cell lysate was used to control for protein expression (lane 1-2 and 5-6). Compared with the negative control (lane 3), a specific band indicates a physical interaction between cystin and necdin (lane 4, arrowhead).</p>", "links"=>[], "tags"=>["cystin", "necdin", "further", "verified", "gst", "pull-down"], "article_id"=>875032, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g002", "stats"=>{"downloads"=>2, "page_views"=>79, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_interaction_between_cystin_and_necdin_was_further_verified_by_GST_pull_down_and_co_immunoprecipitation_/875032", "title"=>"The interaction between cystin and necdin was further verified by GST pull-down and co-immunoprecipitation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311601"], "description"=>"<p>+LgT and Lam+LgT were used as positive and negative controls, respectively. Necdin was switched from the prey vector (pGADT7) to the bait vector (pGBKT7). The new constructs were re-tested and their interactions were validated. 3-AT: 3-amino-1,2,4-triazole, a competitive inhibitor of the His3 protein. p53</p>", "links"=>[], "tags"=>[], "article_id"=>875045, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.t002", "stats"=>{"downloads"=>12, "page_views"=>22, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Vector_switch_to_eliminate_false_positive_clones_/875045", "title"=>"Vector switch to eliminate false positive clones.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311586"], "description"=>"<p>(<b>A</b>) After the initial unbiased screen full-length cystin was cloned into a prey vector, while necdin was cloned into a bait vector. Both were co-transformed and spread onto control SD/-Leu-Trp (data not shown) and selective SD/-Ade-His-Leu-Trp plates. A series of deleted cystin constructs were co-transformed with full-length necdin to isolate the necdin-interacting domain. Y2H positive (pGADT7-LgT+pGBKT7-p53) and negative controls (pGADT7-LgT+pGBKT7-Lam) are also shown. A scheme of the interactions between the versions of cystin and necdin are shown at the lower panel. The C-terminal 25 aa of cystin are required for its interaction with necdin. (<b>B</b>) A series of necdin constructs (prey) were co-transformed along with full-length cystin (bait) to determine the cystin-interacting domain. A scheme of the interaction between the versions of necdin and cystin are shown in the lower panel. Necdins cystin interaction domain lies within aa 71 - 305.</p>", "links"=>[], "tags"=>["cystin", "necdin", "yeast", "two-hybrid"], "article_id"=>875030, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g001", "stats"=>{"downloads"=>0, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_An_interaction_between_cystin_and_necdin_was_identified_in_a_yeast_two_hybrid_screen_/875030", "title"=>"An interaction between cystin and necdin was identified in a yeast two-hybrid screen.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311597"], "description"=>"<p>(<b>A</b>) Immunoblot analysis of c-myc expression in total kidney lysates from 14 day-old <i>Cys1^cpk/cpk</i> (MUT) and wild-type (WT) mice, densitometry shown below. (<b>B</b>) Schematic structures of the <i>Myc</i> P1 and P2 genomic promoter (upper) and the <i>Myc</i> P1 luciferase construct (lower) where <i>Myc</i> P1 DNA from –88 to +47 was cloned into pGL4.22 vector. (<b>C</b>) Luciferase analysis of the effect of necdin and cystin on <i>Myc</i> P1 activity. Basal P1 activity (lane 2) is elevated ∼1.5 fold by necdin (lane 3) and to a lesser extent by cystin alone (lane 4). However, cystin abrogates the ability of necdin to activate the P1 element when co-transfected (lane 6), as long as the necdin interacting domain remains intact [i.e. the –C25 mutant does not inhibit necdin (lane 7)]. Error bars represent the 95% confidence interval for the SEM (p<0.05).</p>", "links"=>[], "tags"=>["activation", "necdin", "p1", "promoter", "antagonized"], "article_id"=>875041, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g006", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_activation_effect_of_necdin_on_Myc_P1_promoter_activity_is_antagonized_by_cystin_/875041", "title"=>"The activation effect of necdin on <i>Myc</i> P1 promoter activity is antagonized by cystin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}
• {"files"=>["https://ndownloader.figshare.com/files/1311595"], "description"=>"<p>A stable cell line transfected with both cystin::GFP and necdin::RFP, was established in mIMCD-3 cells. Under identical conditions, the co-localization of cystin and necdin was determined with and without leptomycin B (LMB) treatment. As shown by epifluorescence, in confluent mIMCD-3 cells, cystin::GFP was primarily retained in the cytoplasm, while necdin::RFP was mainly distributed in the nucleus (I-III). Cystin and necdin only minimally co-localize in the cytoplasm. After LMB treatment (80 nM, 5 hrs lower panels, IV-VI), cystin::GFP was retained in the nucleus and co-localized with necdin (V, white dashed oval).</p>", "links"=>[], "tags"=>["cystin", "necdin", "co-localized", "mimcd-3"], "article_id"=>875039, "categories"=>["Biological Sciences"], "users"=>["Maoqing Wu", "Chaozhe Yang", "Binli Tao", "Su Bu", "Lisa M. Guay-Woodford"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0083062.g005", "stats"=>{"downloads"=>0, "page_views"=>26, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Exogenous_cystin_and_necdin_were_co_localized_in_mIMCD_3_cells_/875039", "title"=>"Exogenous cystin and necdin were co-localized in mIMCD-3 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-12-11 03:50:31"}

PMC Usage Stats | Further Information

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

Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[269, 466, 588, 697, 800, 896, 988, 1076, 1165, 1254, 1340, 1417]}, {"subject_area"=>"/Biology and life sciences/Anatomy", "average_usage"=>[248, 440, 562, 666, 765, 856, 944, 1028, 1112, 1198, 1282, 1362, 1430]}, {"subject_area"=>"/Medicine and health sciences/Anatomy", "average_usage"=>[248, 441, 564, 668, 769, 859, 948, 1034, 1117, 1202, 1290, 1368, 1437]}]}

F1000Prime