Laboratory Andrea Pichler

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Posttranslational modifications are powerful tools to reversibly modulate protein function. They allow dynamic control of cellular processes without de novo protein synthesis. Besides phosphorylation, methylation or acetylation, ubiquitin and its relatives are amongst the most frequently used reversible modifications.

Ubiquitin and SUMO (small ubiquitin related modifier) are small proteins involved in the dynamic regulation of protein function. We investigate the regulation of covalent attachment of these modifiers to their substrates. Modification is performed by an enzymatic cascade of which we are interested in regulation via E2 enzymes in mammalian and yeast cells.


Group Leader

Andrea Pichler
phone: -777

pichler@ie-freiburg.mpg.de

1966
Born in St. Pölten, Austria
undergraduate studies in Biology at University of Vienna, Austria

1998
PhD studies at University of Vienna, Austria

1998- 2005
Postdoctoral fellow at the Novartis Research Institute, Vienna, Austria, at the Max Planck Institute of Biochemistry, Munich and at the University of Göttingen, Germany

2006-2009
Independent Projectleader at the Max F. Perutz Laboratories, Vienna, Austria

Since 2010
Group leader at the Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany

 

Project Areas

  • Regulation of sumoylation by its sole E2 enzyme Ubc9

    Regulation of sumoylation by its sole E2 enzyme Ubc9

    SUMO (small ubiquitin related modifier) is an essential posttranslational modification with roles in most cellular pathways. It is generally conjugated to its...

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  • Regulation of ubiquitination by the E2-enzyme E2-25K

    Regulation of ubiquitination by the E2-enzyme E2-25K

    Ubiquitination regulates thousands of cellular proteins involved in multiple cellular functions requiring a tightly regulated system.

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Recent Publications

Group Members