Phosphorylation of the Yeast γ-Tubulin Tub4 Regulates Microtubule Function
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{"title"=>"Phosphorylation of the yeast γ-tubulin tub4 regulates microtubule function", "type"=>"journal", "authors"=>[{"first_name"=>"Tien chen", "last_name"=>"Lin", "scopus_author_id"=>"39561242800"}, {"first_name"=>"Linda", "last_name"=>"Gombos", "scopus_author_id"=>"14008624500"}, {"first_name"=>"Annett", "last_name"=>"Neuner", "scopus_author_id"=>"35086753100"}, {"first_name"=>"Dominik", "last_name"=>"Sebastian", "scopus_author_id"=>"39561550800"}, {"first_name"=>"Jesper V.", "last_name"=>"Olsen", "scopus_author_id"=>"7403259606"}, {"first_name"=>"Ajla", "last_name"=>"Hrle", "scopus_author_id"=>"37124226100"}, {"first_name"=>"Christian", "last_name"=>"Benda", "scopus_author_id"=>"6603963197"}, {"first_name"=>"Elmar", "last_name"=>"Schiebel", "scopus_author_id"=>"7004819796"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"79955816394", "isbn"=>"1932-6203 (Electronic)\\n1932-6203 (Linking)", "issn"=>"19326203", "pmid"=>"21573187", "pui"=>"361746679", "doi"=>"10.1371/journal.pone.0019700", "scopus"=>"2-s2.0-79955816394"}, "id"=>"2604baa2-d7ba-3542-bb1d-97eee42e00d3", "abstract"=>"The yeast γ-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in γ-tubulins from yeast to human.", "link"=>"http://www.mendeley.com/research/phosphorylation-yeast-%CE%B3tubulin-tub4-regulates-microtubule-function", "reader_count"=>34, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>8, "Student > Ph. D. Student"=>14, "Student > Postgraduate"=>2, "Other"=>2, "Student > Master"=>3, "Student > Bachelor"=>2, "Professor"=>2}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>8, "Student > Ph. D. Student"=>14, "Student > Postgraduate"=>2, "Other"=>2, "Student > Master"=>3, "Student > Bachelor"=>2, "Professor"=>2}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>5, "Agricultural and Biological Sciences"=>28, "Pharmacology, Toxicology and Pharmaceutical Science"=>1}, "reader_count_by_subdiscipline"=>{"Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>28}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>5}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "reader_count_by_country"=>{"Czech Republic"=>1, "Netherlands"=>1, "United States"=>1}, "group_count"=>1}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/777900"], "description"=>"<p>(A-E) <i>TUB4-AID</i> cells with the wild type <i>TUB4</i> (“WT”; A), empty plasmid (“null”; B), <i>tub4-S74E</i> (C), <i>tub-S100E</i> (D) or <i>tub4-S360D</i> (E) were synchronized with α-factor and treated with IAA as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0019700#pone-0019700-g004\" target=\"_blank\">Figure 4A</a>. 75 min after the G1 release cells were prepared for thin serial sectioning electron microscopy as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0019700#s4\" target=\"_blank\">Materials and Methods</a>. (C–D) Shown are two consecutive sections. The white arrows indicate the position of defective nuclear microtubules. Abbreviations: CP, cytoplasm; cMT, cytoplasmic microtubules; N, nucleus; NE, nuclear envelope; nMT, nuclear microtubules; SPB, spindle pole body. Scale bar: 200 nm.</p>", "links"=>[], "tags"=>["microtubule", "phenotype", "cells", "electron"], "article_id"=>448257, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Analysis_of_the_microtubule_phenotype_of_tub4_S74E_tub4_S100E_and_tub4_S360D_cells_by_thin_section_electron_microscopy_/448257", "title"=>"Analysis of the microtubule phenotype of <i>tub4-S74E</i>, <i>tub4-S100E</i> and <i>tub4-S360D</i> cells by thin section electron microscopy.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:17:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/390106", "https://ndownloader.figshare.com/files/390122", "https://ndownloader.figshare.com/files/390129", "https://ndownloader.figshare.com/files/390145", "https://ndownloader.figshare.com/files/390151", "https://ndownloader.figshare.com/files/390159", "https://ndownloader.figshare.com/files/390171", "https://ndownloader.figshare.com/files/390182", "https://ndownloader.figshare.com/files/390194", "https://ndownloader.figshare.com/files/390205"], "description"=>"<div><p>The yeast γ-tubulin Tub4 is assembled with Spc97 and Spc98 into the small Tub4 complex. The Tub4 complex binds via the receptor proteins Spc72 and Spc110 to the spindle pole body (SPB), the functional equivalent of the mammalian centrosome, where the Tub4 complex organizes cytoplasmic and nuclear microtubules. Little is known about the regulation of the Tub4 complex. Here, we isolated the Tub4 complex with the bound receptors from yeast cells. Analysis of the purified Tub4 complex by mass spectrometry identified more than 50 phosphorylation sites in Spc72, Spc97, Spc98, Spc110 and Tub4. To examine the functional relevance of the phosphorylation sites, phospho-mimicking and non-phosphorylatable mutations in Tub4, Spc97 and Spc98 were analyzed. Three phosphorylation sites in Tub4 were found to be critical for Tub4 stability and microtubule organization. One of the sites is highly conserved in γ-tubulins from yeast to human.</p> </div>", "links"=>[], "tags"=>["phosphorylation", "yeast", "tub4", "regulates", "microtubule"], "article_id"=>137035, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0019700.s001", "https://dx.doi.org/10.1371/journal.pone.0019700.s002", "https://dx.doi.org/10.1371/journal.pone.0019700.s003", "https://dx.doi.org/10.1371/journal.pone.0019700.s004", "https://dx.doi.org/10.1371/journal.pone.0019700.s005", "https://dx.doi.org/10.1371/journal.pone.0019700.s006", "https://dx.doi.org/10.1371/journal.pone.0019700.s007", "https://dx.doi.org/10.1371/journal.pone.0019700.s008", "https://dx.doi.org/10.1371/journal.pone.0019700.s009", "https://dx.doi.org/10.1371/journal.pone.0019700.s010"], "stats"=>{"downloads"=>17, "page_views"=>35, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Phosphorylation_of_the_Yeast_Tubulin_Tub4_Regulates_Microtubule_Function/137035", "title"=>"Phosphorylation of the Yeast γ-Tubulin Tub4 Regulates Microtubule Function", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2011-05-05 01:57:15"}
  • {"files"=>["https://ndownloader.figshare.com/files/777319"], "description"=>"<p>(A) SDS-PAGE analysis of the γ-tubulin complex after Gal1-induced expression of <i>SPC97-TAP</i>, <i>SPC98</i> and <i>TUB4</i>. Spc97-TAP was purified with an IgG-Sepharose column. Coomassie Blue staining visualized the core components of the Tub4 complex. (B) MS/MS spectra of the doubly charged phospho-peptides AIMMDSEPSVIADVENTFR (66–84) and NTWVASDGASAGNSWANGYDIGTR (91–114) from Tub4. The red marked serine residues S74 and S100 were identified to be phosphorylated. b- and y-type ions observed in the MS/MS spectra are shown. (C) Diagram summarising the key domain features of Spc97, Spc98, Spc110 and Spc72 and the distribution of the identified phosphorylation sites. The conserved regions (red blocks) of Spc97 and Spc98 were determined by protein sequence alignment of corresponding orthologous proteins from at least seven species (see Figure 1E). DD: dimerization domain; CD: central domain; γ-tubulinBD: γ-tubulin binding domain; GRIP: gamma ring protein domain; γ-TuCBD: γ-tubulin complex binding domain; CC: coiled-coil domain; CBD: calmodulin binding domain. (D) Phosphorylation sites in Tub4. Top: Position of the identified phosphorylation sites (S42, S74, S199, S346 and S415), the cyclin-dependent kinase (Cdk1) consensus site S360 and the GTP binding site in Tub4. Bottom: The 3D structure was generated by ESyPred3D homology modelling using human γ-tubulin crystal structure “3CB2, chain A” as template. Identified phosphorylation sites are shown in red and the cyclin-dependent kinase (CDK) consensus site in blue. (E) Protein sequence alignment of Tub4 with γ-tubulin from other organisms covering the region around residue S360. S360 and the flanking region on Tub4/γ-tubulin are highly conserved and match the minimal consensus motif of Cdk1 (S/T-P) or of Pho85, a cyclin-dependent kinase (S/T-P-X-Ψ, where Ψ is any hydrophobic residue <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0019700#pone.0019700-ONeill1\" target=\"_blank\">[72]</a>).</p>", "links"=>[], "tags"=>["sites", "yeast"], "article_id"=>447681, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g001", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phosphorylation_sites_in_yeast_947_TuSC_/447681", "title"=>"Phosphorylation sites in yeast γ-TuSC.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:08:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/778196"], "description"=>"<p>(A) High gene copy of <i>tub4-S360D</i> restores growth of cells. <i>tub4Δ</i> pRS424-<i>tub4-S360D</i> or <i>tub4Δ tub4-S360E</i> cells grew at 23°C and 30°C but show reduced or no growth at 33°C or 37°C. In contrast, <i>tub4Δ</i> pRS424-<i>tub4-S74E</i> and <i>tub4Δ</i> pRS424-<i>tub4-S100E</i> cells were not viable at 23°C (not shown) or 30°C. (B) Immunoblot blot analysis of yeast cell extracts from <i>TUB4-5FLAG</i> cells carrying the indicated mutant <i>tub4</i> alleles on the 2 µm plasmid pRS424. The upper blot was developed with anti-Tub4 antibodies. The anti-actin blot was used as loading control. (C) Quantification of the signals of (B). The graph shows the quantification of anti-Tub4-FLAG and anti-Tub4 signals from three independent experiments, normalized to actin levels. Shown is the mean of Tub4 levels with standard deviation. Significance of the difference between wild type and mutants at <i>p</i><0.05 was determined by one-way ANOVA and is indicated by an asterisk. (D) Immunoblot blot analysis of yeast cell extracts from YPH499 <i>TUB4</i> wild type cells, and <i>tub4Δ</i> cells with 2 µm-<i>TUB4</i> (“WT”), 2 µm-<i>tub4-S360D</i> and 2 µm-<i>tub4-S360E</i>. The anti-actin blot was used as loading control. (E) Quantification of the signals of (D). The graph shows the quantification of anti-Tub4 signals from three independent experiments, normalized to actin levels. Shown is the mean of Tub4 levels with standard deviation. Significance of the difference between YPH499 and 2 µm strains at <i>p</i><0.05 was determined by one-way ANOVA and is indicated by an asterisk.</p>", "links"=>[], "tags"=>["tub4-s360d", "restores"], "article_id"=>448555, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g007", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overexpression_of_tub4_S360D_restores_viability_/448555", "title"=>"Overexpression of tub4-S360D restores viability.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:22:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/778358"], "description"=>"<p>(A) <i>TUB4-AID SPC42-GFP</i> cells with the empty plasmid pRS305 (null), or <i>TUB4</i> (WT), <i>tub4-S74E</i>, <i>tub4-S100E</i> or <i>tub4-S360D</i> on the integration plasmid pRS305 were incubated with IAA to induce degradation of Tub4-AID. Cells were fixed and then analyzed by indirect immunofluorescence for Tub4 at SPBs. DNA was stained with DAPI. Scale bar: 5 µm. (B) Quantification of the Tub4 SPB signal of cells from (A). Signal intensities were background-subtracted and normalized against the Spc42-GFP signal. Significance of the difference between wild-type and mutant Tub4 signals (p<0.001) was determined by one-way ANOVA and is indicated by an asterisk. (C and D) <i>TUB4-AID SPC42-mCherry SPC97-GFP</i> cells and <i>TUB4-AID SPC42-GFP SPC110-mCherry</i> cells with the empty plasmid pRS305 (“null”), or <i>TUB4</i> (WT), <i>tub4-S74E</i>, <i>tub4-S100E</i> and <i>tub4-S360D</i> on the integration plasmid pRS305 were incubated with IAA to induce degradation of Tub4-AID. Spc97-GFP and Spc110-mCherry signals at SPBs were determined with fluorescence microscopy and then quantified. (S) Significance of the difference between wild-type and mutants at p<0.05 was determined by one-way ANOVA and is indicated by an asterisk. RI: relative intensity.</p>", "links"=>[], "tags"=>["localization", "tub4-s100e"], "article_id"=>448717, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g008", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SPB_localization_of_Tub4_S74E_Tub4_S100E_and_Tub4_S360D_/448717", "title"=>"SPB localization of Tub4-S74E, Tub4-S100E and Tub4-S360D.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:25:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/778039"], "description"=>"<p>(Ai) In the presence of Tub4-6HA cellular levels of the phospho-mimicking Tub4-S74E, Tub4-S100E and Tub4-S360D are similar to Tub4. Lysates from <i>SPC97 TUB4-6HA</i> cells (strain YPH499; lane 1), and cells of <i>SPC97-5FLAG TUB4-6HA</i> with pRS305 (lane 2), pRS305-<i>TUB4</i> (lane 3), pRS305-<i>tub4-S74E</i> (lane 4), pRS305-<i>tub4-S100E</i> (lane 5), pRS305-<i>tub4-S360A</i> (lane 6) and pRS305-<i>tub4-S360D</i> (lane 7) were used for anti-FLAG and anti-Tub4 immunoblots. (Aii) Lysates of cells from (Ai) were subjected to immunoprecipitation with anti-FLAG antibodies. Tub4-6HA, Tub4 and Spc98 were analyzed for co-immunoprecipitation using anti-Spc98 and anti-Tub4 antibodies. (Aiii) Anti-HA immunoprecipitations using cells lysates from (Ai). The immunoprecipitations were analyzed with anti-Tub4 and anti-FLAG antibodies. Input is 5% of the immunoprecipitation input. (B) <i>TUB4-AID SPC97-3HA</i> cells carrying pRS305 (“null”) or <i>TUB4</i> (“WT”), <i>tub4-S74E</i>, <i>tub4-S100E</i> or <i>tub4-S360D</i> on integration vector pRS305 were incubated with IAA for 2 h at 30°C to induce degradation of Tub4-AID. Degradation of Tub4-AID in the presence of IAA was confirmed by immunoblotting (top panel). Lysates of <i>SPC97</i> wild type cells incubated in the presence of IAA were subjected to anti-HA IP as negative control (“neg”) to exclude non-specific binding of proteins to beads. The IPs were analyzed by immunoblotting with anti-Tub4, anti-Spc98, anti-Spc110 and anti-HA (Spc97-3HA blot) antibodies. Anti-actin antibodies were used to normalize loading. (C) Tub4-S360D and Spc98 levels were reduced in the absence of wild-type Tub4-AID activity. Input protein levels of cleared cell extracts from (B) were quantified and normalized for actin. The normalized value of wild-type Tub4 cells was set to one. Mean and standard deviation of at least three independent cell extracts are shown. Significance of the difference between wild-type and mutants at <i>p</i><0.05 was determined by one-way ANOVA and is indicated by an asterisk. (D) Phospho-mimicking mutations in Tub4 affect binding to Spc110. Quantified protein levels of Tub4 complex proteins and Spc110 in the Spc97-3HA immunoprecipitations were normalized to precipitated Spc97-3HA. The normalized value of wild-type Tub4 was set as one. Mean and standard deviations of at least three independent samples are shown. Significance of the difference between wild-type and mutants at <i>p</i><0.05 was determined by one-way ANOVA and is indicated by an asterisk. RI: relative intensity.</p>", "links"=>[], "tags"=>["alleles", "tub4", "components"], "article_id"=>448401, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g006", "stats"=>{"downloads"=>2, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phospho_mimicking_tub4_S74E_tub4_S100E_and_tub4_S360D_alleles_affect_the_interaction_between_Tub4_complex_components_and_Spc110_/448401", "title"=>"Phospho-mimicking <i>tub4-S74E</i>, <i>tub4-S100E</i> and<i>tub4-S360D</i> alleles affect the interaction between Tub4 complex components and Spc110.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:20:01"}
  • {"files"=>["https://ndownloader.figshare.com/files/777473"], "description"=>"<p>(A) Growth assay showing that <i>tub4-S74E, tub4-S100E</i> and <i>tub4-S360D/E</i> cells are lethal. The <i>tub4Δ</i> pRS316-<i>TUB4</i> shuffle strain was transformed with <i>LEU2</i>-based plasmids (pRS315) containing various <i>TUB4</i> alleles. Transformants were grown on SC-Leu or 5-FOA plates for three days at 30°C. 5-FOA only allows cells to grow that have lost the <i>URA3</i>-based pRS316-<i>TUB4</i>. Thus, in cells that grown on 5-FOA plates, the pRS315 encoded <i>TUB4</i> allele is the only source of Tub4 activity. (B) <i>tub4-S100A</i> genetically interacts with <i>mad2Δ</i>. <i>tub4-S100A mad2Δ</i> cells showed a temperature-sensitive growth defect at 37°C.</p>", "links"=>[], "tags"=>["microbiology", "cell biology", "biophysics", "Biochemistry"], "article_id"=>447828, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g002", "stats"=>{"downloads"=>2, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_tub4_S74E_tub4_S100E_and_tub4_S360D_E_cells_are_lethal_/447828", "title"=>"<i>tub4-S74E</i>, <i>tub4-S100E</i>and<i>tub4-S360D/E</i>cells are lethal.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:10:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/777716"], "description"=>"<p>(A) <i>TUB4-AID</i> cells with empty vector (“null”), <i>TUB4</i> (“WT”), <i>tub4-S74E</i>, <i>tub4-S100E</i> or <i>tub4-S360D</i> were arrested in G1-phase with α-factor. IAA was added 30 min before G1 release by washing cells with YPAD containing IAA (G1 release t = 0). Cells were fixed at the indicated time points with paraformaldehyde. DNA was stained with DAPI and cells were analyzed by fluorescence microscopy. <i>SPC42-mCherry</i> is a SPB marker; <i>GFP-TUB1</i> encodes the yeast α-tubulin gene. N>150 cells per time point were categorized as indicated. (B) Spindle phenotypes of <i>tub4-S74E</i>, <i>tub4-S100E</i> and <i>tub4-S360D</i> cells. Cells of (A) were sampled 75 min after G1 release and analyzed by fluorescence microscopy. Scale bar: 10 µm. (C) Quantification of phenotypes of cells in (B) 75 min after G1 release. N>100 cells per mutant were analyzed as indicated in the figure. (D) Time dependent changes of null, <i>tub4-S74E</i>, <i>tub4-S100E</i> and <i>tub4-S360D</i> cells from (A) with monopolar spindle, metaphase-like spindle and short bipolar spindle and long cMTs. N>150 cells per time point. (E) Length of metaphase-like spindles over time. Metaphase-like cells from (A) were analyzed for spindle length. The spindle length of Gal1-<i>CDC20</i> cells was used as reference (N >100 with the exception of <i>tub4-S100E</i> cells where N was 41). The significance of the difference between Gal1-<i>CDC20</i> cells and mutants at <i>p</i><0.05 was determined by one-way ANOVA. (F) <i>tub4-S74E, tub4-S100E</i> and <i>tub4-S360D</i> cells with a short bipolar spindle showed longer cytoplasmic microtubules than metaphase arrested Gal1-<i>CDC20</i> cells. <i>TUB4-AID</i> cells from (A) were sampled 75 min after G1 release. The length of the cytoplasmic microtubules (distance from the SPB to cell cortex) was determined from 3D reconstitution of cells. <i>tub4-S74E, tub4-S100E</i> and <i>tub4-S360D</i> cells showed longer cytoplasmic microtubules in comparison to wild-type and metaphase-arrested Gal1-<i>CDC20</i> cells (n>100). Significance of the difference between wild-type and mutants at <i>p</i><0.05 was determined by one-way ANOVA and is indicated by an asterisk.</p>", "links"=>[], "tags"=>["mutant", "cells", "abnormal"], "article_id"=>448081, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g004", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phospho_mimicking_tub4_S74E_tub4_S100E_and_tub4_S360D_mutant_cells_have_abnormal_microtubules_/448081", "title"=>"Phospho-mimicking <i>tub4-S74E</i>, <i>tub4-S100E</i> and <i>tub4-S360D</i> mutant cells have abnormal microtubules.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:14:41"}
  • {"files"=>["https://ndownloader.figshare.com/files/777595"], "description"=>"<p>(A) <i>TUB4-AID</i> cells with empty integration vector pRS305 (“null”) or pRS305 with <i>TUB4</i> (“WT”), <i>tub4-S74E</i>, <i>tub4-S100E</i> or <i>tub4-S360D</i> were grown on YPD or YPD plates with IAA at 23°C. (B) Western blot analysis of <i>TUB4-AID</i> cells with anti-Tub4 antibodies after the addition of IAA (t = 0). The lower molecular weight band (“Control”) is a protein that cross reacts with the anti-Tub4 antibodies and was used as loading control.</p>", "links"=>[], "tags"=>["degradation"], "article_id"=>447960, "categories"=>["Biochemistry", "Cell Biology", "Microbiology", "Biophysics"], "users"=>["Tien-chen Lin", "Linda Gombos", "Annett Neuner", "Dominik Sebastian", "Jesper V. Olsen", "Ajla Hrle", "Christian Benda", "Elmar Schiebel"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0019700.g003", "stats"=>{"downloads"=>3, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Auxin_induced_degradation_of_Tub4_/447960", "title"=>"Auxin-induced degradation of Tub4.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-05-05 02:12:40"}

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  • {"unique-ip"=>"10", "full-text"=>"9", "pdf"=>"16", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
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  • {"unique-ip"=>"10", "full-text"=>"6", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"6", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
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Relative Metric

{"start_date"=>"2011-01-01T00:00:00Z", "end_date"=>"2011-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[290, 559, 698, 813, 927, 1028, 1121, 1206, 1289, 1360, 1433, 1501, 1569, 1637, 1707, 1774, 1841, 1911, 1974, 2038, 2103, 2161, 2219, 2280, 2345, 2406, 2466, 2529, 2592, 2654, 2713, 2772, 2835, 2893, 2954, 3020, 3071]}, {"subject_area"=>"/Biology and life sciences/Cell biology", "average_usage"=>[289, 559, 699, 817, 931, 1031, 1127, 1214, 1297, 1370, 1444, 1515, 1584, 1656, 1726, 1797, 1862, 1930, 1996, 2061, 2125, 2190, 2250, 2311, 2373, 2435, 2496, 2563, 2630, 2692, 2760, 2824, 2898, 2960, 3019, 3089, 3143]}]}
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