The Mitotic Arrest Deficient Protein MAD2B Interacts with the Small GTPase RAN throughout the Cell Cycle
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{"title"=>"The mitotic arrest deficient protein MAD2B interacts with the small GTPase RAN throughout the cell cycle", "type"=>"journal", "authors"=>[{"first_name"=>"Klaas", "last_name"=>"Medendorp", "scopus_author_id"=>"23005674600"}, {"first_name"=>"Jan J.M.", "last_name"=>"van Groningen", "scopus_author_id"=>"6603850350"}, {"first_name"=>"Lilian", "last_name"=>"Vreede", "scopus_author_id"=>"22942568500"}, {"first_name"=>"Lisette", "last_name"=>"Hetterschijt", "scopus_author_id"=>"33367711800"}, {"first_name"=>"Wilhelmina H.", "last_name"=>"van den Hurk", "scopus_author_id"=>"6602683653"}, {"first_name"=>"Diederik R.H.", "last_name"=>"de Bruijn", "scopus_author_id"=>"6701328806"}, {"first_name"=>"Linda", "last_name"=>"Brugmans", "scopus_author_id"=>"35180980800"}, {"first_name"=>"Ad Geurts", "last_name"=>"van Kessel", "scopus_author_id"=>"35460415400"}], "year"=>2009, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "doi"=>"10.1371/journal.pone.0007020", "pui"=>"355296598", "sgr"=>"70349266555", "pmid"=>"19753112", "scopus"=>"2-s2.0-70349266555"}, "id"=>"aa5da47f-7357-3aaf-aefd-6c690f24abc9", "abstract"=>"BACKGROUND: Previously, we identified the mitotic arrest deficient protein MAD2B (MAD2L2) as a bona fide interactor of the renal cell carcinoma (RCC)-associated protein PRCC. In addition, we found that fusion of PRCC with the transcription factor TFE3 in t(X;1)(p11;q21)-positive RCCs results in an impairment of this interaction and, concomitantly, an abrogation of cell cycle progression. Although MAD2B is thought to inhibit the anaphase promoting complex (APC) by binding to CDC20 and/or CDH1(FZR1), its exact role in cell cycle control still remains to be established. METHODOLOGY/PRINCIPAL FINDINGS: Using a yeast two-hybrid interaction trap we identified the small GTPase RAN, a well-known cell cycle regulator, as a novel MAD2B binding protein. Endogenous interaction was established in mammalian cells via co-localization and co-immunoprecipitation of the respective proteins. The interaction domain of RAN could be assigned to a C-terminal moiety of 60 amino acids, whereas MAD2B had to be present in its full-length conformation. The MAD2B-RAN interaction was found to persist throughout the cell cycle. During mitosis, co-localization at the spindle was observed. CONCLUSIONS/SIGNIFICANCE: The small GTPase RAN is a novel MAD2B binding protein. This novel protein-protein interaction may play a role in (i) the control over the spindle checkpoint during mitosis and (ii) the regulation of nucleocytoplasmic trafficking during interphase.", "link"=>"http://www.mendeley.com/research/mitotic-arrest-deficient-protein-mad2b-interacts-small-gtpase-ran-throughout-cell-cycle", "reader_count"=>19, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Researcher"=>5, "Student > Ph. D. Student"=>7, "Student > Master"=>1, "Other"=>1, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Researcher"=>5, "Student > Ph. D. Student"=>7, "Student > Master"=>1, "Other"=>1, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>11, "Medicine and Dentistry"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>11}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Canada"=>1, "Mexico"=>1}, "group_count"=>0}

Scopus | Further Information

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  • {"files"=>["https://ndownloader.figshare.com/files/883854"], "description"=>"<p>(A) U2OS cells expressing HA-MAD2B protein were lysed and probed for interaction with either GST-RAN or GST alone. Specific interaction between MAD2B and RAN was detected by western blot analysis using an anti-MAD2B antibody. (B, C) COS-1 cells were transiently transfected with MAD2B, RAN or both as indicated on top. Immunoprecipitations were performed with pre-mouse serum (M IgG), pre-rabbit serum (R IgG), anti-MAD2B and anti-RAN antibodies as indicated. Western blot analyses were performed with (B) an anti-MAD2B antibody, and (C) an anti-RAN-antibody. The positions of the immunoreactive MAD2B and RAN proteins are marked on the right. The (co-)immunoprecipitated MAD2B (B) and RAN (C) proteins are marked with arrowheads. The background bands represent immunoglobulin heavy and light chains, respectively. (D) Immunoprecipitations were carried out with an anti-MAD2B antibody and a control rabbit antibody (IgG) on HeLa cell lysates as indicated. Western blots analyses were performed with an anti-RAN (upper panel) and an anti-MAD2B (lower panel) antibody, respectively. (E) COS-1 cells were transiently transfected with FLAG-MAD2B protein and FLAG-tagged deletion constructs of MAD2B as indicated (see also <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0007020#pone-0007020-g001\" target=\"_blank\">Fig. 1</a>). Upper panel: immunoprecipitations with an anti-RAN antibody, lower panel: input lysates. The background bands in the upper panel represent immunoglobulin light chains. Western blot analyses were performed with an anti-FLAG antibody. (F) COS-1 cells were transiently transfected with MAD2B and immunoprecipitations were performed with anti-RAN and anti-H-RAS antibodies, respectively. A pre-mouse serum (IgG) was included as a negative control. Western blot analysis was performed with an anti-MAD2B antibody.</p>", "links"=>[], "tags"=>["mad2b", "ran"], "article_id"=>554304, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Klaas Medendorp", "Jan J. M. van Groningen", "Lilian Vreede", "Lisette Hetterschijt", "Wilhelmina H. van den Hurk", "Diederik R. H. de Bruijn", "Linda Brugmans", "Ad Geurts van Kessel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0007020.g002", "stats"=>{"downloads"=>3, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Co_immunoprecipitation_of_MAD2B_and_RAN_proteins_/554304", "title"=>"Co-immunoprecipitation of MAD2B and RAN proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-09-15 01:11:44"}
  • {"files"=>["https://ndownloader.figshare.com/files/883984"], "description"=>"<p>Endogenous MAD2B, RAN and γ-tubulin (mitotic spindle) are shown in green, red and white, respectively. DAPI staining (blue) was used to mark nuclei and chromosomes. The overlay of the different signals (Merge) reveals a near perfect co-localization of the respective proteins at the mitotic spindle (arrows). Images were captured using confocal laser scanning microscopy.</p>", "links"=>[], "tags"=>["mad2b"], "article_id"=>554436, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Klaas Medendorp", "Jan J. M. van Groningen", "Lilian Vreede", "Lisette Hetterschijt", "Wilhelmina H. van den Hurk", "Diederik R. H. de Bruijn", "Linda Brugmans", "Ad Geurts van Kessel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0007020.g003", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sub_cellular_co_localization_of_MAD2B_and_RAN_/554436", "title"=>"Sub-cellular (co-)localization of MAD2B and RAN.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-09-15 01:13:56"}
  • {"files"=>["https://ndownloader.figshare.com/files/438186", "https://ndownloader.figshare.com/files/438208"], "description"=>"<div><h3>Background</h3><p>Previously, we identified the mitotic arrest deficient protein MAD2B (MAD2L2) as a <em>bona fide</em> interactor of the renal cell carcinoma (RCC)-associated protein PRCC. In addition, we found that fusion of PRCC with the transcription factor TFE3 in t(X;1)(p11;q21)-positive RCCs results in an impairment of this interaction and, concomitantly, an abrogation of cell cycle progression. Although MAD2B is thought to inhibit the anaphase promoting complex (APC) by binding to CDC20 and/or CDH1(FZR1), its exact role in cell cycle control still remains to be established.</p><h3>Methodology/Principal Findings</h3><p>Using a yeast two-hybrid interaction trap we identified the small GTPase RAN, a well-known cell cycle regulator, as a novel MAD2B binding protein. Endogenous interaction was established in mammalian cells via co-localization and co-immunoprecipitation of the respective proteins. The interaction domain of RAN could be assigned to a C-terminal moiety of 60 amino acids, whereas MAD2B had to be present in its full-length conformation. The MAD2B-RAN interaction was found to persist throughout the cell cycle. During mitosis, co-localization at the spindle was observed.</p><h3>Conclusions/Significance</h3><p>The small GTPase RAN is a novel MAD2B binding protein. This novel protein-protein interaction may play a role in (i) the control over the spindle checkpoint during mitosis and (ii) the regulation of nucleocytoplasmic trafficking during interphase.</p></div>", "links"=>[], "tags"=>["mitotic", "deficient", "mad2b", "interacts", "gtpase", "ran"], "article_id"=>146390, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Klaas Medendorp", "Jan J. M. van Groningen", "Lilian Vreede", "Lisette Hetterschijt", "Wilhelmina H. van den Hurk", "Diederik R. H. de Bruijn", "Linda Brugmans", "Ad Geurts van Kessel"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0007020.s001", "https://dx.doi.org/10.1371/journal.pone.0007020.s002"], "stats"=>{"downloads"=>0, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Mitotic_Arrest_Deficient_Protein_MAD2B_Interacts_with_the_Small_GTPase_RAN_throughout_the_Cell_Cycle/146390", "title"=>"The Mitotic Arrest Deficient Protein MAD2B Interacts with the Small GTPase RAN throughout the Cell Cycle", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2009-09-15 01:46:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/883753"], "description"=>"<p>Schematic representation of the MAD2B full length protein and deletion constructs (numbers correspond to amino acid positions) used in the assay and the capacity of the respective co-transfected yeast cells to grow on selective medium (-HALW). The presence of β-galactosidase activity (β-gal) as measured in filter lift assays is indicated by +.</p>", "links"=>[], "tags"=>["two-hybrid", "ran", "mad2b", "deletion"], "article_id"=>554202, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Klaas Medendorp", "Jan J. M. van Groningen", "Lilian Vreede", "Lisette Hetterschijt", "Wilhelmina H. van den Hurk", "Diederik R. H. de Bruijn", "Linda Brugmans", "Ad Geurts van Kessel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0007020.g001", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Yeast_two_hybrid_analysis_of_full_length_RAN_with_MAD2B_deletion_constructs_/554202", "title"=>"Yeast two-hybrid analysis of full length RAN with MAD2B deletion constructs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-09-15 01:10:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/884169"], "description"=>"<p>U2OS cells were transiently (co-)transfected with MAD2B-CFP (green), PRCC-dsRed (red) and/or RAN-YFP (yellow) expression constructs. The overlay of the different signals (Merge) reveals a partial co-localization of the respective proteins. Images were captured using fluorescence microscopy.</p>", "links"=>[], "tags"=>["ran", "prcc", "u2os"], "article_id"=>554618, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Klaas Medendorp", "Jan J. M. van Groningen", "Lilian Vreede", "Lisette Hetterschijt", "Wilhelmina H. van den Hurk", "Diederik R. H. de Bruijn", "Linda Brugmans", "Ad Geurts van Kessel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0007020.g005", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sub_cellular_co_localization_of_MAD2B_RAN_and_PRCC_in_U2OS_cells_/554618", "title"=>"Sub-cellular (co-)localization of MAD2B, RAN and PRCC in U2OS cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-09-15 01:16:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/884078"], "description"=>"<p>COS-1 cells were transiently transfected with MAD2B, blocked at different phases in the cell cycle and, subsequently, released from these cell cycle blocks during different time intervals. (1) cells isolated from a confluent culture, (2) cells isolated 3 h after 1∶2 splitting of a confluent culture, (3) cells blocked with nocodazole, (4) cells blocked with nocodazole and released for 4 h, (5) cells blocked with nocodazole and released for 8 h, (6) cells blocked with hydroxyurea, and (7) cells blocked with hydroxyurea and released for 6 h. (A) FACS profiles confirming the presence of the cells in the different phases of the cell cycle are shown. (B) Western blot analysis of total lysates with anti-RAN, anti-MAD2B and anti-γ-tubulin antibodies (Input) and after anti-RAN immunoprecipitation of the respective lysates (1–7) using an anti-MAD2B antibody (IP).</p>", "links"=>[], "tags"=>["ran"], "article_id"=>554527, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Klaas Medendorp", "Jan J. M. van Groningen", "Lilian Vreede", "Lisette Hetterschijt", "Wilhelmina H. van den Hurk", "Diederik R. H. de Bruijn", "Linda Brugmans", "Ad Geurts van Kessel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0007020.g004", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAD2B_and_RAN_interact_throughout_the_cell_cycle_/554527", "title"=>"MAD2B and RAN interact throughout the cell cycle.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-09-15 01:15:27"}

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