Mardo Kõivomägi "Studies on the substrate specificity and multisite phosphorylation mechanisms of cyclin-dependent kinase Cdk1 in Saccharomyces cerevisiae" | University of Tartu

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Contacts of UT units

Faculty of Arts and Humanities
Faculty phone: 
+372 737 5341
Faculty address: 
Jakobi 2, rooms 116–121, 51005 Tartu
  • Dean's Office
    Faculty phone: 
    + 372 737 5341
    Faculty address: 
    Jakobi 2, rooms 116–121, 51005 Tartu
  • Institute of History and Archaeology
    Faculty phone: 
    +372 737 5651
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    Jakobi 2, 51005 Tartu
  • Institute of Estonian and General Linguistics
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    Faculty address: 
    Jakobi 2, 51005 Tartu
  • Institute of Philosophy and Semiotics
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    Faculty address: 
    Jakobi 2, rooms 309–352, 51005 Tartu
  • Institute of Cultural Research
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    Ülikooli 16, 51003 Tartu
  • School of Theology and Religious Studies
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    +372 737 5301
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    Ülikooli 18–310, 50090 Tartu
  • College of Foreign Languages and Cultures
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    Lossi 3, 51003 Tartu
  • Viljandi Culture Academy
    Faculty phone: 
    +372 435 5232
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    Posti 1, 71004 Viljandi
Faculty of Social Sciences
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+372 737 5957
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Lossi 36, 51003 Tartu
  • Dean's Office
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    + 372 737 5900
    Faculty address: 
    Lossi 36, 51003 Tartu
  • Institute of Education
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    Faculty address: 
    Salme 1a–29, 50103 Tartu
  • Johan Skytte Institute of Political Studies
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    Lossi 36–301, 51003 Tartu
  • School of Economics and Business Administration
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  • Institute of Psychology
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  • Institute of Biomedicine and Translational Medicine
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    Faculty address: 
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    Narva mnt 18, 51009 Tartu
  • Estonian Marine Institute
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    Mäealuse 14, 12618 Tallinn
  • Institute of Physics
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    Vanemuise 46, 51003 Tartu
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    W. Struve 1, 50091 Tartu
  • Youth Academy
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    Faculty address: 
    Uppsala 10, 51003 Tartu
  • Institute of Genomics
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    Faculty address: 
    Riia 23b, 51010 Tartu
  • Museum
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    Lossi 25, 51003 Tartu
  • University of Tartu Natural History Museum and Botanical Garden
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    Faculty address: 
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  • University Office in Tallinn
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  • Estates Office
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Mardo Kõivomägi "Studies on the substrate specificity and multisite phosphorylation mechanisms of cyclin-dependent kinase Cdk1 in Saccharomyces cerevisiae"

Date: 
15.03.2013 - 15:00 to 17:00

Supervisor: vanemteadur Mart Loog (Tartu Ülikool)
Opponent: Dr. Jan M. Skotheim, PhD, Department of Biology, Stanford University, Stanford, California, USA.

Summary:
The cell cycle is the process by which cells duplicate their contents and then divide to produce a pair of daughter cells. The master regulators of the cell cycle are cyclin dependent kinases (CDKs). CDKs are activated by their perio¬dically accumulating regulatory partners, the cyclins. The enzymatic activity of cyclin-Cdk complexes is tightly controlled by a variety of mechanisms. Sub¬strate targeting by a given cyclin-Cdk complex is mediated by the active site on the CDK and docking sites on the cyclin subunits. Additionally, the presence of a phosphate-binding pocket on the CDK adaptor subunit Cks1 promotes inter¬action with targets containing multiple phosphorylation sites. In simple euka¬ryotes, such as budding yeast, a single CDK, Cdk1, enzyme associates with se¬veral different cyclins. The combination of rising levels of CDK activity and the distinct substrate specificities of different cyclin-Cdk complexes enables the tem¬porally ordered phosphorylation of the many target proteins that regulate cell cycle events. Robust inhibition of S-phase CDK activity in the G1 phase of the cell cycle is the major mechanism preventing uncontrolled onset of DNA replication. In budding yeast, S phase is switched on after the rapid proteolytic degradation of the Cdk1 inhibitor Sic1. Sic1 is a stoichometric inhibitor of Clb-Cdk1 comple¬xes. It appears at the end of mitosis, and its destruction at the G1/S boundary is induced by Cdk1-mediated multisite phosphorylation. The first part of the present dissertation provides an overview of cell cycle control systems, focusing on the different substrate specificities of the various cyclin-Cdk complexes. Next, the CDK inhibitors in yeast and mammalian cells are introduced. Finally, the role of Cks1 as a phosphate binding adaptor mole¬cule for CDK, and the functional implications of this role are reviewed. The original results presented here cover the following areas: a) studies and discus-sions on the changes in cyclin-Cdk1 substrate specificity during the cell cycle b) in vivo and in vitro characterization and analysis of multisite phosphorylation of Sic1, and c) characterization of the parameters promoting Cks1-mediated multi-site phosphorylation of Cdk1 targets.

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