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  • 1
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    Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-05
    Description: The COP9 signalosome is an evolutionary conserved multiprotein complex of unknown function that acts as a negative regulator of photomorphogenic seedling development in Arabidopsis. Here, we show that plants with reduced COP9 signalosome levels had decreased auxin response similar to loss-of-function mutants of the E3 ubiquitin ligase SCFTIR1. Furthermore, we found that the COP9 signalosome and SCFTIR1 interacted in vivo and that the COP9 signalosome was required for efficient degradation of PSIAA6, a candidate substrate of SCFTIR1. Thus, the COP9 signalosome may play an important role in mediating E3 ubiquitin ligase-mediated responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwechheimer, C -- Serino, G -- Callis, J -- Crosby, W L -- Lyapina, S -- Deshaies, R J -- Gray, W M -- Estelle, M -- Deng, X W -- New York, N.Y. -- Science. 2001 May 18;292(5520):1379-82. Epub 2001 May 3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11337587" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/*drug effects/enzymology/genetics/growth & development ; Brassica ; Darkness ; Gene Expression Regulation, Plant/drug effects ; Genes, Reporter/genetics ; Indoleacetic Acids/*pharmacology ; Ligases/genetics/*metabolism ; Multiprotein Complexes ; Mutation/genetics ; Peas ; Peptide Hydrolases ; Phenotype ; Plant Proteins/genetics/*metabolism ; Plant Roots/drug effects/enzymology/genetics/growth & development ; Plants, Genetically Modified ; Precipitin Tests ; Protein Binding ; Protein Biosynthesis ; Protein Subunits ; Proteins/genetics/*metabolism ; RNA, Antisense/genetics ; RNA, Plant/genetics/metabolism ; Two-Hybrid System Techniques ; Ubiquitin-Protein Ligases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-05
    Description: SCF ubiquitin ligases control various processes by marking regulatory proteins for ubiquitin-dependent proteolysis. To illuminate how SCF complexes are regulated, we sought proteins that interact with the human SCF component CUL1. The COP9 signalosome (CSN), a suppressor of plant photomorphogenesis, associated with multiple cullins and promoted cleavage of the ubiquitin-like protein NEDD8 from Schizosaccharomyces pombe CUL1 in vivo and in vitro. Multiple NEDD8-modified proteins uniquely accumulated in CSN-deficient S. pombe cells. We propose that the broad spectrum of activities previously attributed to CSN subunits--including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export--underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lyapina, S -- Cope, G -- Shevchenko, A -- Serino, G -- Tsuge, T -- Zhou, C -- Wolf, D A -- Wei, N -- Deshaies, R J -- New York, N.Y. -- Science. 2001 May 18;292(5520):1382-5. Epub 2001 May 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11337588" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Blotting, Western ; Cell Cycle Proteins/genetics/*metabolism ; *Cullin Proteins ; Fungal Proteins/genetics/metabolism ; HeLa Cells ; Humans ; Mass Spectrometry ; Mice ; Multiprotein Complexes ; Mutation/genetics ; Peptide Hydrolases ; Peptide Synthases/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Protein Subunits ; Proteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; SKP Cullin F-Box Protein Ligases ; Schizosaccharomyces/genetics/metabolism ; Substrate Specificity ; Swine ; Transfection ; Two-Hybrid System Techniques ; Ubiquitins/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif-EX(n)HXHX(10)D. Mutation of the predicted active-site histidines to alanine (rpn11AXA) was lethal and stabilized ubiquitin pathway substrates in yeast. Rpn11(AXA) mutant proteasomes assembled normally but failed to either deubiquitinate or degrade ubiquitinated Sic1 in vitro. Our findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, Rati -- Aravind, L -- Oania, Robert -- McDonald, W Hayes -- Yates, John R 3rd -- Koonin, Eugene V -- Deshaies, Raymond J -- RR11823-05-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):611-5. Epub 2002 Aug 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183636" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Carbon-Nitrogen Lyases/chemistry/*metabolism ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cysteine Endopeptidases/metabolism ; DNA-Binding Proteins/chemistry ; Endopeptidases/chemistry/*metabolism ; Fungal Proteins/*metabolism ; Metalloendopeptidases/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; Mutation ; Oligopeptides/pharmacology ; Peptide Hydrolases/*metabolism ; Proteasome Endopeptidase Complex ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Transcription Factors/chemistry ; Ubiquitins/*metabolism ; Yeasts/metabolism ; Zinc/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Drug discovery: Fresh target for cancer therapy (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deshaies, Raymond J -- England -- Nature. 2009 Apr 9;458(7239):709-10. doi: 10.1038/458709a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19360071" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/*therapeutic use ; *Drug Discovery ; Humans ; Neoplasms/*drug therapy ; Proteins/metabolism ; Ubiquitins/therapeutic use
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    Gal4 turnover and transcription activation (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-10-09
    Description: Growing evidence supports the notion that proteasome-mediated destruction of transcriptional activators can be intimately coupled to their function. Recently, Nalley et al. challenged this view by reporting that the prototypical yeast activator Gal4 does not dynamically associate with chromatin, but rather 'locks in' to stable promoter complexes that are resistant to competition. Here we present evidence that the assay used to reach this conclusion is unsuitable, and that promoter-bound, active Gal4 is indeed susceptible to competition in vivo. Our data challenge the key evidence that Nalley et al. used to reach their conclusion, and indicate that Gal4 functions in vivo within the context of dynamic promoter complexes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3072683/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3072683/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collins, Galen A -- Lipford, J Russell -- Deshaies, Raymond J -- Tansey, William P -- P01 CA013106/CA/NCI NIH HHS/ -- P01 CA013106-310027/CA/NCI NIH HHS/ -- England -- Nature. 2009 Oct 8;461(7265):E7; discussion E8. doi: 10.1038/nature08406.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Watson School of Biological Sciences, 1 Bungtown Road, Cold Spring Harbor, New York 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19812621" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive/drug effects ; Chromatin Immunoprecipitation ; DNA-Binding Proteins/*metabolism ; Estradiol/pharmacology ; Galactokinase/genetics ; Promoter Regions, Genetic/genetics ; Protein Binding/drug effects ; Receptors, Estrogen/agonists/chemistry/metabolism ; Reproducibility of Results ; Research Design ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Tamoxifen/analogs & derivatives/pharmacology ; Trans-Activators/genetics ; Transcription Factors/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    Detection of sequential polyubiquitylation on a millisecond timescale (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-12-04
    Description: The pathway by which ubiquitin chains are generated on substrate through a cascade of enzymes consisting of an E1, E2 and E3 remains unclear. Multiple distinct models involving chain assembly on E2 or substrate have been proposed. However, the speed and complexity of the reaction have precluded direct experimental tests to distinguish between potential pathways. Here we introduce new theoretical and experimental methodologies to address both limitations. A quantitative framework based on product distribution predicts that the really interesting new gene (RING) E3 enzymes SCF(Cdc4) and SCF(beta-TrCP) work with the E2 Cdc34 to build polyubiquitin chains on substrates by sequential transfers of single ubiquitins. Measurements with millisecond time resolution directly demonstrate that substrate polyubiquitylation proceeds sequentially. Our results present an unprecedented glimpse into the mechanism of RING ubiquitin ligases and illuminate the quantitative parameters that underlie the rate and pattern of ubiquitin chain assembly.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2791906/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2791906/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pierce, Nathan W -- Kleiger, Gary -- Shan, Shu-ou -- Deshaies, Raymond J -- GM065997/GM/NIGMS NIH HHS/ -- R01 GM065997/GM/NIGMS NIH HHS/ -- R01 GM065997-07/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2009 Dec 3;462(7273):615-9. doi: 10.1038/nature08595.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Division of Biology, MC 156-29, Pasadena, California 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19956254" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemistry/*methods ; Humans ; Kinetics ; Models, Chemical ; SKP Cullin F-Box Protein Ligases/metabolism ; Time Factors ; Ubiquitin-Activating Enzymes/metabolism ; Ubiquitination/*physiology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 7
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    Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-23
    Description: G1 cyclin-dependent kinase (Cdk)-triggered degradation of the S-phase Cdk inhibitor Sic1p has been implicated in the transition from G1 to S phase in the cell cycle of budding yeast. A multidimensional electrospray mass spectrometry technique was used to map G1 Cdk phosphorylation sites in Sic1p both in vitro and in vivo. A Sic1p mutant lacking three Cdk phosphorylation sites did not serve as a substrate for Cdc34p-dependent ubiquitination in vitro, was stable in vivo, and blocked DNA replication. Moreover, purified phosphoSic1p was ubiquitinated in cyclin-depleted G1 extract, indicating that a primary function of G1 cyclins is to tag Sic1p for destruction. These data suggest a molecular model of how phosphorylation and proteolysis cooperate to bring about the G1/S transition in budding yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, R -- Annan, R S -- Huddleston, M J -- Carr, S A -- Reynard, G -- Deshaies, R J -- R01 GM52466-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):455-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, Box 156-29, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase-Promoting Complex-Cyclosome ; Cyclin G ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/*metabolism ; DNA Replication ; Enzyme Inhibitors/metabolism ; Fungal Proteins/*metabolism ; G1 Phase ; Ligases/metabolism ; Molecular Sequence Data ; Mutagenesis ; Phenotype ; Phosphopeptides/metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; *S Phase ; *Saccharomyces cerevisiae Proteins ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; Yeasts/*cytology/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-02
    Description: To identify previously unknown small molecules that inhibit cell cycle machinery, we performed a chemical genetic screen in Xenopus extracts. One class of inhibitors, termed ubistatins, blocked cell cycle progression by inhibiting cyclin B proteolysis and inhibited degradation of ubiquitinated Sic1 by purified proteasomes. Ubistatins blocked the binding of ubiquitinated substrates to the proteasome by targeting the ubiquitin-ubiquitin interface of Lys(48)-linked chains. The same interface is recognized by ubiquitin-chain receptors of the proteasome, indicating that ubistatins act by disrupting a critical protein-protein interaction in the ubiquitin-proteasome system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, Rati -- Peters, Noel R -- D'Onofrio, Mariapina -- Tochtrop, Gregory P -- Sakamoto, Kathleen M -- Varadan, Ranjani -- Zhang, Mingsheng -- Coffino, Philip -- Fushman, David -- Deshaies, Raymond J -- King, Randall W -- CA78048/CA/NCI NIH HHS/ -- GM068276/GM/NIGMS NIH HHS/ -- GM65334/GM/NIGMS NIH HHS/ -- GM66492/GM/NIGMS NIH HHS/ -- P50 CA92131/CA/NCI NIH HHS/ -- R01 GM-45335/GM/NIGMS NIH HHS/ -- R21CA108545/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 1;306(5693):117-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Howard Hughes Medical Institute (HHMI), California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15459393" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase-Promoting Complex-Cyclosome ; Animals ; Cell Extracts ; Cyclin B/metabolism ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cysteine Endopeptidases/metabolism ; *Drug Evaluation, Preclinical ; Interphase ; Mitosis ; Molecular Structure ; Multienzyme Complexes/*antagonists & inhibitors/metabolism ; Ornithine Decarboxylase/metabolism ; Proteasome Endopeptidase Complex ; Protein Binding ; Proteins/*metabolism ; Quinolines/*metabolism/pharmacology ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins/metabolism ; Sulfanilic Acids/*metabolism/pharmacology ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligase Complexes/metabolism ; Xenopus laevis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-24
    Description: Arabidopsis thaliana De-etiolated-1 (AtDET1) is a highly conserved protein, with orthologs in vertebrate and invertebrate organisms. AtDET1 negatively regulates photomorphogenesis, but its biochemical mechanism and function in other species are unknown. We report that human DET1 (hDET1) promotes ubiquitination and degradation of the proto-oncogenic transcription factor c-Jun by assembling a multisubunit ubiquitin ligase containing DNA Damage Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1 (ROC1), and constitutively photomorphogenic-1. Ablation of any subunit by RNA interference stabilized c-Jun and increased c-Jun-activated transcription. These findings characterize a c-Jun ubiquitin ligase and define a specific function for hDET1 in mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wertz, Ingrid E -- O'Rourke, Karen M -- Zhang, Zemin -- Dornan, David -- Arnott, David -- Deshaies, Raymond J -- Dixit, Vishva M -- GM065997/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Feb 27;303(5662):1371-4. Epub 2004 Jan 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, Inc., South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739464" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cloning, Molecular ; Cullin Proteins/genetics/*metabolism ; DNA-Binding Proteins/metabolism ; Genes, jun ; Humans ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/metabolism ; Protein Binding ; Proteomics ; Proto-Oncogene Proteins c-jun/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Small Interfering/metabolism ; Transfection ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/chemistry/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Phosphorylation by cyclin B-Cdk underlies release of mitotic exit activator Cdc14 from the nucleolus (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-27
    Description: Budding yeast protein phosphatase Cdc14 is sequestered in the nucleolus in an inactive state during interphase by the anchor protein Net1. Upon entry into anaphase, the Cdc14 early anaphase release (FEAR) network initiates dispersal of active Cdc14 throughout the cell. We report that the FEARnetwork promotes phosphorylation of Net1 by cyclin-dependent kinase (Cdk) complexed with cyclin B1 or cyclin B2. These phosphorylations appear to be required for FEAR and sustain the proper timing of late mitotic events. Thus, a regulatory circuit exists to ensure that the arbiter of the mitotic state, Cdk, sets in motion events that culminate in exit from mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Azzam, Ramzi -- Chen, Susan L -- Shou, Wenying -- Mah, Angie S -- Alexandru, Gabriela -- Nasmyth, Kim -- Annan, Roland S -- Carr, Steven A -- Deshaies, Raymond J -- GM59940/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 23;305(5683):516-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15273393" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Cell Cycle Proteins/genetics/*metabolism ; Cell Nucleolus/*metabolism ; Cyclin B/metabolism ; Cyclin B1 ; Cyclin-Dependent Kinases/*metabolism ; DNA, Ribosomal/metabolism ; Meiosis ; Metaphase ; *Mitosis ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Protein Tyrosine Phosphatases/*metabolism ; Protein-Serine-Threonine Kinases ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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