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{"title"=>"Analysis of Protein Phosphatase-1 and Aurora Protein Kinase Suppressors Reveals New Aspects of Regulatory Protein Function in Saccharomyces cerevisiae", "type"=>"journal", "authors"=>[{"first_name"=>"Anuprita", "last_name"=>"Ghosh", "scopus_author_id"=>"55803148700"}, {"first_name"=>"John F.", "last_name"=>"Cannon", "scopus_author_id"=>"7201637531"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "pmid"=>"23894419", "pui"=>"369412098", "scopus"=>"2-s2.0-84880647930", "doi"=>"10.1371/journal.pone.0069133", "sgr"=>"84880647930"}, "id"=>"bf344f2b-c3b3-35ed-9ca0-b35e8598e166", "abstract"=>"Protein phosphatase-1 (PP1) controls many processes in eukaryotic cells. Modulation of mitosis by reversing phosphorylation of proteins phosphorylated by aurora protein kinase is a critical function for PP1. Overexpression of the sole PP1, Glc7, in budding yeast, Saccharomyces cerevisiae, is lethal. This work shows that lethality requires the function of Glc7 regulatory proteins Sds22, Reg2, and phosphorylated Glc8. This finding shows that Glc7 overexpression induced cell death requires a specific subset of the many Glc7-interacting proteins and therefore is likely caused by promiscuous dephosphorylation of a variety of substrates. Additionally, suppression can occur by reducing Glc7 protein levels by high-copy Fpr3 without use of its proline isomerase domain. This divulges a novel function of Fpr3. Most suppressors of GLC7 overexpression also suppress aurora protein kinase, ipl1, temperature-sensitive mutations. However, high-copy mutant SDS22 genes show reciprocal suppression of GLC7 overexpression induced cell death or ipl1 temperature sensitivity. Sds22 binds to many proteins besides Glc7. The N-terminal 25 residues of Sds22 are sufficient to bind, directly or indirectly, to seven proteins studied here including the spindle assembly checkpoint protein, Bub3. These data demonstrate that Sds22 organizes several proteins in addition to Glc7 to perform functions that counteract Ipl1 activity or lead to hyper Glc7 induced cell death. These data also emphasize that Sds22 targets Glc7 to nuclear locations distinct from Ipl1 substrates.", "link"=>"http://www.mendeley.com/research/analysis-protein-phosphatase1-aurora-protein-kinase-suppressors-reveals-new-aspects-regulatory-prote", "reader_count"=>29, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>18, "Student > Master"=>3, "Professor"=>3}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>3, "Student > Ph. D. Student"=>18, "Student > Master"=>3, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>7, "Agricultural and Biological Sciences"=>19, "Medicine and Dentistry"=>1, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>19}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>7}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Germany"=>1}, "group_count"=>1}

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• http://doi.org/10.1016/j.fgb.2016.06.003
• http://doi.org/10.3390/ijms21207733
• http://doi.org/10.1534/genetics.114.161224
• http://doi.org/10.1093/nar/gkw168
• http://doi.org/10.1016/j.str.2018.12.002
• http://doi.org/10.1093/nar/gkx1180
• http://doi.org/10.1534/genetics.119.302235
• http://doi.org/10.1016/j.bbamcr.2020.118727

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/1125059"], "description"=>"<p><b>A)</b> Structure of wild-type and mutant Sds22 proteins. Residue numbers are listed on top. Rectangles show the extents of 10.5 leucine-rich repeats. Mutant proteins diagramed below have asterisks for missense mutations and parentheses showing the extent of deletions, which removed whole repeats and maintained reading frame. Function of each mutant protein was assessed by complementation of <i>sds22Δ</i> by high-copy mutant genes. JC1378 (<i>sds22Δ::HIS3/+</i>) was transformed with 2μ <i>URA3 SDS22-X-myc3</i> plasmids, sporulated and at least 20 tetrads dissected. Complementation was indicated by viable His⁺ spore clones. Only <i>SDS22-D273A</i> could complement. <b>B, C, D)</b> Fivefold serial dilutions of JC1126-15B transformed with high-copy <i>SDS22</i> genes with the indicated genotypes was incubated on <i>-</i>Ura plates at the indicated temperatures. The <i>SDS22-RM12</i> gene, which suffered a large deletion, serves as a negative control. <b>E)</b> Anti-Myc antibody probed immunoblot of crude extracts of JC1126-15B transformants with high-copy <i>SDS22-X-myc</i> plasmids or pRS316 (empty). Molecular masses in kDa are shown on left. Pgk1 levels in these extracts are shown at the bottom as control.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "high-copy", "mutant"], "article_id"=>750176, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g005", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Suppression_of_ipl1_by_high_copy_SDS22_mutant_genes_/750176", "title"=>"Suppression of <i>ipl1</i> by high-copy <i>SDS22</i> mutant genes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125061"], "description"=>"<p><b>A)</b> JC746-9D transformants with pRS314 (odd rows) or pYT251 (<i>GAL1p-GLC7</i>, even rows) and plasmids with the indicated genotypes were grown on selective galactose or glucose plates. <b>B)</b> JC746-9D/pYT251 additionally transformed with pRS314, pAG108, p2757, or pAG-RM45 were grown on selective galactose or glucose plates. <b>C)</b> JC746-9D/pYT251 transformants with plasmid combinations pRS426+ pRS315 (control), pAG108+ pRS315 (<i>SDS22</i>), pRS426+ p2752 (<i>SDS22-RM45</i>), or pAG108+ p2752 (<i>SDS22 SDS22-RM45</i>) were grown on selective glucose or galactose plates. For all panels, fivefold serial dilutions were spotted on plated and grown for three days.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "suppression", "mutant"], "article_id"=>750178, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g006", "stats"=>{"downloads"=>1, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dominant_GLC7_suppression_by_mutant_SDS22_/750178", "title"=>"Dominant <i>GLC7</i> suppression by mutant <i>SDS22</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125062"], "description"=>"<p><b>A)</b> GST fusion proteins were purified from JC746-9D transformed with p2518 (HA3-Sds22) or p2757 (HA3-Sds22-RM45) and indicated GST fusions as described (<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0069133#s4\" target=\"_blank\">Materials and Methods</a>). The immunoblot of crude extracts probed with anti-GST antibody in top image. The arrows point to full-length proteins or specific degradation product. Immunoblots of the affinity-purified GST fusion mixture probed with anti-HA antibody in bottom images. <b>B)</b> Two-hybrid assay of Sds22 interaction with Glc7. The β-galactosidase activity of three independent PJ69-4A transformants with pAS1-<i>GLC7</i> and indicated Gal4AD-Sds22 fusions were assayed. The control is transformed with pRS315. The average and standard deviation is reported. Immunoblots of crude extracts probed with anti-Gal4AD antibody showed equivalent Gal4AD-Sds22 expression for each mutant fusion protein. The Sds22-S56am and RM45 fusions produced β-galactosidase activity that was comparable to the negative control. In contrast, every other fusion had activity significantly higher (two-tailed t-test, p<0.01).</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "binding"], "article_id"=>750179, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g007", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sds22_binding_proteins_/750179", "title"=>"Sds22 binding proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125064"], "description"=>"<p>JC1624 (<i>GAL1p-lacZ</i>)/pRS314 (<b>A, </b><b>B and D</b>) or JC1353-17B/p2603 (<i>SDS22(1–25)-lacZ</i> ) (<b>C</b>) were transformed with plasmids expressing indicated GST fusion proteins. <b>A)</b> The GST-fusion proteins in affinity purified GST fusion protein complexes probed with anti-GST antibody. A 55 kDa background antigen is present in all lanes. Ygr130C-specific bands are visible on longer exposure. <b>B)</b> Crude extract of JC1624/pRS314 probed with anti-β-galactosidase antibody. The JC1353-17B/p2603 crude extracts looked similar, but had a slower migration and 60-fold lower expression (data not shown). <b>C)</b> Sds22(1–25)-LacZ bound to GST fusion proteins in JC1353-17B/p2603 detected with anti-β-galactosidase antibody. This exposure is intentionally long to visualize the signal from the Ahc1 negative control. Only Bub3, Kog1, Rvb1, Rvb2, and Snf4 gave a greater signal than Ahc1. <b>D)</b> β-galactosidase bound to GST fusion proteins in JC1624/pRS314 detected with anti-β-galactosidase antibody. When overexpressed like panel C, all lanes have equal signal. In panels <b>B–D</b>, the “−” lane is JC1353-17B/pRS314 crude extract and the “+” lane is JC1353-17B/p2603 crude extract.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "binding"], "article_id"=>750181, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g008", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Proteins_binding_to_Sds22_1_8211_25_LacZ_/750181", "title"=>"Proteins binding to Sds22(1–25)-LacZ.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125065"], "description"=>"<p>Yeast strains used in this work.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "strains"], "article_id"=>750182, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.t002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Yeast_strains_used_in_this_work_/750182", "title"=>"Yeast strains used in this work.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125066"], "description"=>"<p>Plasmids used in this work.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division"], "article_id"=>750183, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.t003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Plasmids_used_in_this_work_/750183", "title"=>"Plasmids used in this work.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125067"], "description"=>"*<p>The seven other Sds22 binding proteins are Bub3, Kog1, Nop6, Rvb1, Rvb2, Snf4, and Ygr130C. The five Sds22-S56am-binding proteins are Bub3, Kog1, Rvb1, Rvb2, and Snf4 (missing Nop6 and Ygr130C). This is based on Sds22(1–25)-LacZ affinity (<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0069133#pone-0069133-g008\" target=\"_blank\"><b>Figure 8</b></a>).</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "suppression"], "article_id"=>750184, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.t001", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_suppression_by_SDS22_genes_/750184", "title"=>"Summary of suppression by <i>SDS22</i> genes.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125051"], "description"=>"<p><b>A)</b> JC746-9D (wt), JFY183 (<i>gac1</i>), JC1287-1C (<i>reg1</i>), JC938-5C (<i>glc8</i>), and JC1583 (<i>reg2</i>) transformed with <i>GAL1p-GLC7</i> plasmids, p2562 or pKC978 (even rows) or control plasmids pRS315 or pRS316 (odd rows) were grown in selective raffinose medium and then serial five-fold dilutions were spotted on –Ura or –Leu glucose, YEP-galactose, or –Ura or –Leu galactose plates. <b>B)</b> Phospho-Glc8 is required for Glc7 overexpression lethality. JC938-5C (<i>glc8</i>) transformed with pYT251 (<i>GAL1p-GLC7</i>) and either p1945 (<i>GLC8</i>), pYT115 (<i>GLC8-T118A</i>), or p1614 (<i>GAL1p-GLC8</i>) were grown on –Trp –Ura galactose (Gal) or glucose (Glc). <b>C)</b> Diploids JC746, JC746/V76B8, JC746/RG200 and JC1378 transformed with pYT251 (<i>GAL1p-GLC7</i>) or pRS314 (control) were grown on –Trp galactose. The <i>SDS22</i> genotypes of the host strains are shown. In all panels, the galactose medium induced <i>GLC7</i> expression from the <i>GAL1</i> promoter.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "suppressors", "glc7"], "article_id"=>750172, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g001", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Recessive_suppressors_of_Glc7_overexpression_/750172", "title"=>"Recessive suppressors of Glc7 overexpression.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125053"], "description"=>"<p><b>A)</b> JC746-9D/pYT251 (<i>GAL1p-GLC7</i>) transformed with high-copy plasmids p2509 (<i>FPR3</i>), p2510 (<i>FPR4</i>), p2613 <i>(Δ121-167)</i>, p2615 (<i>K302oc</i>), or p2431 (<i>SDS22</i>) grown in –Trp –Ura raffinose were serially diluted and spotted on a –Trp –Ura glucose or galactose plate. The relevant genotypes of the plasmids are indicated. <b>B)</b> Domains of Fpr3. The asterisk indicates Tyr-184, which is phosphorylated by casein kinase-2 <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0069133#pone.0069133-Wilson1\" target=\"_blank\">[78]</a>. The peptidylprolyl isomerase (PPI) domain location is based on homology to other yeast proline isomerases.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "suppressors", "glc7"], "article_id"=>750173, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dominant_suppressors_of_Glc7_overexpression_/750173", "title"=>"Dominant suppressors of Glc7 overexpression.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125055"], "description"=>"<p>Crude extracts of SBY625/pRS426 (lanes 1-3), SBY625/p2509 (lanes 4–6), W303-1A (lane 7), SBY625 (<i>GLC7-HA3</i>) (lanes 8, 9), JC1552-17A (lane 10), JC1535 (lane 11), JC746-9D/YCp50 (lane 12), JC746-9D/YCp50-HA-GLC7 (lane 13), JC1338-20A/YCp50 (lane 14), and JC1338-20A/YCp50-HA-GLC7 (lane 15) were separated by SDS-PAGE, blotted and probed with anti-HA or anti-Pgk1 antibodies. All lanes except lane 9 have 20 µg protein,which has 10 µg. All cultures except those in lanes 7–11 were grown in minimal medium; those in lanes 7–11 were grown in YEP-glucose. The pRS426 and p2509 transformants (lanes 1–6) were induced with the indicated final concentration of CuSO₄ during the last two hours of growth. The Glc7/Pgk1 ratio was calculated from film densitometry.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "fpr3", "glc7"], "article_id"=>750174, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g003", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_High_Fpr3_levels_reduce_Glc7_levels_/750174", "title"=>"High Fpr3 levels reduce Glc7 levels.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}
• {"files"=>["https://ndownloader.figshare.com/files/1125057"], "description"=>"<p><b>A)</b> Suppression of <i>ipl1</i> by several high-copy genes. JC1126-15B (<i>ipl1-1</i>) transformed with plasmids (pRS426, p2665, p2509, p2510, p2615, and p2613 respectively) with the indicated genotypes were incubated on –Ura plates at the indicated temperatures. Each spot had approximately 10⁵ cells. <b>B)</b><i>SDS22-RM45</i> is not a dominant suppressor of <i>ipl1</i>. Homozygous <i>ipl1</i> diploid strains, JC1630 (<i>SDS22/SDS22</i>) and JC1631 (<i>SDS22/SDS22Δ</i>) transformed with pRS316 (control), pAG108 (<i>SDS22</i>), or pAG-RM45 (<i>SDS22-RM45</i>) were incubated on –Ura plates at the indicated temperatures. <b>C)</b> Suppression of <i>ipl1</i> by high-copy <i>SDS22-S56am</i>. JC1126-15B transformed with pAG108 (<i>SDS22</i>) or p2665 (<i>SDS22-S56am</i>) were incubated on –Ura plates at the indicated temperatures. Fivefold serial dilutions were spotted and grown for three days in panels <b>B</b> and <b>C</b>.</p>", "links"=>[], "tags"=>["genetics", "Gene function", "Genetic screens", "Molecular genetics", "Molecular cell biology", "Signal transduction", "Mechanisms of signal transduction", "Signal termination", "Signaling in cellular processes", "Mitotic signaling", "Signaling pathways", "cell division", "suppressors"], "article_id"=>750175, "categories"=>["Biological Sciences"], "users"=>["Anuprita Ghosh", "John F. Cannon"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0069133.g004", "stats"=>{"downloads"=>1, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dominant_suppressors_of_ipl1_/750175", "title"=>"Dominant suppressors of <i>ipl1</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-22 02:38:53"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime