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  • 1
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    Identification of a cullin homology region in a subunit of the anaphase-promoting complex (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: The anaphase-promoting complex is composed of eight protein subunits, including BimE (APC1), CDC27 (APC3), CDC16 (APC6), and CDC23 (APC8). The remaining four human APC subunits, APC2, APC4, APC5, and APC7, as well as human CDC23, were cloned. APC7 contains multiple copies of the tetratrico peptide repeat, similar to CDC16, CDC23, and CDC27. Whereas APC4 and APC5 share no similarity to proteins of known function, APC2 contains a region that is similar to a sequence in cullins, a family of proteins implicated in the ubiquitination of G1 phase cyclins and cyclin-dependent kinase inhibitors. The APC2 gene is essential in Saccharomyces cerevisiae, and apc2 mutants arrest at metaphase and are defective in the degradation of Pds1p. APC2 and cullins may be distantly related members of a ubiquitin ligase family that targets cell cycle regulators for degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, H -- Peters, J M -- King, R W -- Page, A M -- Hieter, P -- Kirschner, M W -- CA16519/CA/NCI NIH HHS/ -- GM26875-17/GM/NIGMS NIH HHS/ -- GM39023-08/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1219-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469815" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc2 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc4 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc5 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc7 Subunit, Anaphase-Promoting Complex-Cyclosome ; Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome ; Cell Cycle/*physiology ; Cell Cycle Proteins/chemistry ; Cloning, Molecular ; *Cullin Proteins ; Helminth Proteins/chemistry ; Humans ; Ligases/*chemistry/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Phylogeny ; Proteins/chemistry ; Saccharomyces cerevisiae/chemistry/cytology/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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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
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    How proteolysis drives the cell cycle (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: Oscillations in the activity of cyclin-dependent kinases (CDKs) promote progression through the eukaryotic cell cycle. This review examines how proteolysis regulates CDK activity-by degrading CDK activators or inhibitors-and also how proteolysis may directly trigger the transition from metaphase to anaphase. Proteolysis during the cell cycle is mediated by two distinct ubiquitin-conjugation pathways. One pathway, requiring CDC34, initiates DNA replication by degrading a CDK inhibitor. The second pathway, involving a large protein complex called the anaphase-promoting complex or cyclosome, initiates chromosome segregation and exit from mitosis by degrading anaphase inhibitors and mitotic cyclins. Proteolysis therefore drives cell cycle progression not only by regulating CDK activity, but by directly influencing chromosome and spindle dynamics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, R W -- Deshaies, R J -- Peters, J M -- Kirschner, M W -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1652-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939846" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Anaphase-Promoting Complex-Cyclosome ; Animals ; *Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Division ; Cyclin-Dependent Kinases/antagonists & inhibitors/*metabolism ; Cyclins/metabolism ; Enzyme Inhibitors/metabolism ; Fungal Proteins/metabolism ; Fungi/cytology/metabolism ; G1 Phase ; Humans ; Ligases/metabolism ; Mitosis ; Proteins/*metabolism ; S Phase ; Ubiquitin-Conjugating Enzymes ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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