A Dual Binding Mode for RhoGTPases in Plexin Signalling
Publication Date
August 30, 2011
Journal
PLOS Biology
Authors
Christian H. Bell, A. Radu Aricescu, E. Yvonne Jones & Christian Siebold
Volume
9
Issue
8
Pages
e1001134
DOI
https://dx.plos.org/10.1371/journal.pbio.1001134
Publisher URL
http://journals.plos.org/plosbiology/article?id=10.1371%2Fjournal.pbio.1001134
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/21912513
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166162
Europe PMC
http://europepmc.org/abstract/MED/21912513
Web of Science
000294483000016
Scopus
80052339290
Mendeley
http://www.mendeley.com/research/dual-binding-mode-rhogtpases-plexin-signalling
Events
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Mendeley | Further Information

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Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/740743"], "description"=>"<p>(a) Binding constants (<i>K</i><sub>d</sub>) measured by SPR between different Plexin-B1 constructs carrying mutations in binding site B, and Rac1* and Rnd1, respectively. Data are expressed as mean ± standard error. (b) Histogram showing the effect of different site B mutations on semaphorin-induced collapse. Results are shown as mean with error bars representing standard error of the mean. (c) Sequence alignment of residues involved in site B interaction. Residues that were mutated in the cell collapse assay are marked with a triangle and those that were analysed in both SPR and cellular assays are marked with a dot.</p>", "links"=>[], "tags"=>["binding"], "article_id"=>411121, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1001134.g003", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Characterization_of_the_second_binding_site_/411121", "title"=>"Characterization of the second binding site.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-08-30 00:18:41"}
  • {"files"=>["https://ndownloader.figshare.com/files/740520"], "description"=>"<p>Structure of the monomeric Plexin-B1<sub>Δ1</sub>-Rac1* complex.</p>", "links"=>[], "tags"=>["monomeric"], "article_id"=>410898, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1001134.g001", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_of_the_monomeric_Plexin_B1_916_1_Rac1_complex_/410898", "title"=>"Structure of the monomeric Plexin-B1<sub>Δ1</sub>-Rac1* complex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-08-30 00:14:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/740647"], "description"=>"<p>(a) Overview of the 3-fold arrangement of the three Plexin-B1<sub>cyto</sub>-Rac1* units. Rac1* is coloured in wheat, orange, and yellow, and Plexin-B1<sub>cyto</sub> is coloured in skyblue, paleblue, and palecyan, respectively. GppNHp is shown as spheres. Termini for Rac1* are labelled in the left panel, and termini for Plexin-B1<sub>cyto</sub> in the right panel. α-helices 13, 14, and 15 harbouring the putative Ras-binding site are highlighted in red. (b) Schematic overview of the complex. The orientation and colour coding is as in (a), right panel. The two Rac1 binding sites, site A and site B, are marked by arrowheads. (c) Detailed view of the Rac1 binding site B. The orientation of the left panel is similar to <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001134#pbio-1001134-g001\" target=\"_blank\">Figure 1b</a>, right panel. The three boxed panels correspond to the close-up views depicted in the left panel. Colour coding is as in (a).</p>", "links"=>[], "tags"=>["3-fold"], "article_id"=>411028, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1001134.g002", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_of_the_3_fold_Plexin_B1_cyto_Rac1_complex_/411028", "title"=>"Structure of the 3-fold Plexin-B1<sub>cyto</sub>-Rac1 complex.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-08-30 00:17:08"}
  • {"files"=>["https://ndownloader.figshare.com/files/741005"], "description"=>"a<p>Numbers in parenthesis are for the highest resolution shell.</p>b<p>R<sub>free</sub> equals the R<sub>work</sub> against 5% of the data removed prior to refinement.</p>", "links"=>[], "tags"=>["refinement"], "article_id"=>411382, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1001134.t001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Data_collection_and_refinement_statistics_/411382", "title"=>"Data collection and refinement statistics.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-08-30 00:23:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/740929"], "description"=>"<p>We propose that the Ras-GAP activity of Plexin-B1 is a result of a two-step signalling process. Step one would consist of Rnd1 binding to the intracellular Plexin-B1 RBD region. Binding of Ras molecules to this complex cannot result in GTPase activity unless a second binding event, involving extracellular semaphorin-mediated plexin clustering, induces formation of the intracellular 3-fold Plexin-B1-Rnd1 complexes. Such an arrangement is stabilised by the interaction of Rnd1 with a novel binding site on a neighbouring Plexin-B1 molecule, exposed following the displacement of a juxtamembrane helix at the N-terminal of the plexin intracellular region. In this clustered arrangement RasGAP activity can occur and Ras gets inactivated. The trimer on the inside, in conjunction with semaphorin-plexin dimers on the extracellular side, may lead to the formation of an extended signalling array. R-Ras/M-Ras (Ras) and Rnd1 (Rnd) are depicted in their GTP-bound form. Plexin-B1<sub>cyto</sub> is depicted in blue rectangle, with sites A and B highlighted. The mobile juxtamembrane helix at the N-terminal of the plexin intracellular region is indicated by a red disc. The two GTPases are shown as orange ovals (Rnd1) and green diamonds (Ras), respectively. Semaphorin induced dimerization of the plexin ectodomain is indicated by black lines.</p>", "links"=>[], "tags"=>["intracellular", "plexin"], "article_id"=>411303, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1001134.g005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Model_for_intracellular_plexin_signalling_/411303", "title"=>"Model for intracellular plexin signalling.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-08-30 00:21:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/374881", "https://ndownloader.figshare.com/files/374918", "https://ndownloader.figshare.com/files/374942", "https://ndownloader.figshare.com/files/374990", "https://ndownloader.figshare.com/files/375025", "https://ndownloader.figshare.com/files/375047", "https://ndownloader.figshare.com/files/375086", "https://ndownloader.figshare.com/files/375107", "https://ndownloader.figshare.com/files/375134", "https://ndownloader.figshare.com/files/375166", "https://ndownloader.figshare.com/files/375196"], "description"=>"<div><p>Plexins are cell surface receptors for the semaphorin family of cell guidance cues. The cytoplasmic region comprises a Ras GTPase-activating protein (GAP) domain and a RhoGTPase binding domain. Concomitant binding of extracellular semaphorin and intracellular RhoGTPase triggers GAP activity and signal transduction. The mechanism of this intricate regulation remains elusive. We present two crystal structures of the human Plexin-B1 cytoplasmic region in complex with a constitutively active RhoGTPase, Rac1. The structure of truncated Plexin-B1-Rac1 complex provides no mechanism for coupling RhoGTPase and Ras binding sites. On inclusion of the juxtamembrane helix, a trimeric structure of Plexin-B1-Rac1 complexes is stabilised by a second, novel, RhoGTPase binding site adjacent to the Ras site. Site-directed mutagenesis combined with cellular and biophysical assays demonstrate that this new binding site is essential for signalling. Our findings are consistent with a model in which extracellular and intracellular plexin clustering events combine into a single signalling output.</p> </div>", "links"=>[], "tags"=>["dual", "binding", "rhogtpases", "plexin", "signalling"], "article_id"=>134024, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>["https://dx.doi.org/10.1371/journal.pbio.1001134.s001", "https://dx.doi.org/10.1371/journal.pbio.1001134.s002", "https://dx.doi.org/10.1371/journal.pbio.1001134.s003", "https://dx.doi.org/10.1371/journal.pbio.1001134.s004", "https://dx.doi.org/10.1371/journal.pbio.1001134.s005", "https://dx.doi.org/10.1371/journal.pbio.1001134.s006", "https://dx.doi.org/10.1371/journal.pbio.1001134.s007", "https://dx.doi.org/10.1371/journal.pbio.1001134.s008", "https://dx.doi.org/10.1371/journal.pbio.1001134.s009", "https://dx.doi.org/10.1371/journal.pbio.1001134.s010", "https://dx.doi.org/10.1371/journal.pbio.1001134.s011"], "stats"=>{"downloads"=>3, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/A_Dual_Binding_Mode_for_RhoGTPases_in_Plexin_Signalling/134024", "title"=>"A Dual Binding Mode for RhoGTPases in Plexin Signalling", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2011-08-30 01:07:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/740836"], "description"=>"<p>(a) Superposition of mouse Plexin-A3 (PDB ID: 3IG3) onto the 3-fold Plexin-B1<sub>cyto</sub>-Rac1* complex. Colour coding is as in <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001134#pbio-1001134-g002\" target=\"_blank\">Figure 2a</a>. Plexin-A3 is shown in pale green. The juxtamembrane helix ordered in the Plexin-A3 structure would block Rac1* binding to site B. (b) Representative plots of the equilibrium binding response against Rho GTPase concentration ranging from 120 nM to 2,000 µM. ND, not determinable. The plexin constructs used in each experiment are schematically presented on the right with colour coding as in <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001134#pbio-1001134-g005\" target=\"_blank\">Figure 5</a>.</p>", "links"=>[], "tags"=>["n-terminal", "juxtamembrane"], "article_id"=>411211, "categories"=>["Molecular Biology", "Biochemistry", "Neuroscience"], "users"=>["Christian H. Bell", "A. Radu Aricescu", "E. Yvonne Jones", "Christian Siebold"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1001134.g004", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Analysis_of_the_Plexin_B1_cyto_N_terminal_juxtamembrane_helix_/411211", "title"=>"Analysis of the Plexin-B1<sub>cyto</sub> N-terminal juxtamembrane helix.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-08-30 00:20:11"}

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Relative Metric

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