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Silke Wiesner



Our group studies the molecular mechanisms underlying cell signaling and in particular protein ubiquitylation using NMR spectroscopy, X-ray crystallography and biochemical methods. Many proteins localize in the cell to specific compartments and function only for a limited amount of time. To remove mislocalized or no longer required proteins ubiquitin, a ~10 kD protein, is attached to these proteins. The ubiquitylation reaction involves three enzymes whose exact catalytic mechanisms are unknown. Mutations in ubiquitylation enzymes give rise to severe cellular dysfunctions that cause numerous human diseases including cancer. We seek to understand how ubiquitylation enzymes function on an atomic level, how their activities are controlled and how ubiquitylation regulates cellular behavior.


Key Publications

Aichem A, Anders S, Catone N, Rößler P, Stotz S, Berg A, Schwab R, Scheuermann S, Bialas J, Schütz-Stoffregen MC, Schmidtke G, Peter C, Groettrup M, Wiesner S. The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation. Nat Commun. 2018 9(1):3321. doi: 10.1038/s41467-018-05776-3. PMID: 30127417

Renschler FA, Bruekner SR, Salomon PL, Mukherjee A, Kullmann L, Schütz-Stoffregen MC, Henzler C, Pawson T, Krahn MP, Wiesner S. Structural basis for the interaction between the cell polarity proteins Par3 and Par6. Sci Signal. 2018 Feb 13;11(517). pii: eaam9899. doi: 10.1126/scisignal.aam9899. PMID: 29440511

Stoffregen MC, Schwer MM, Renschler FA, Wiesner S. Methionine scanning as an NMR tool for detecting and analyzing biomolecular interaction surfaces. Structure. 2012 Apr 4;20(4):573-81. doi: 10.1016/j.str.2012.02.012. PMID: 22483105

Wiesner S, Ogunjimi AA, Wang HR, Rotin D, Sicheri F, Wrana JL, Forman-Kay JD. Auto-inhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain. Cell. 2007 Aug 24;130(4):651-62. doi: 10.1016/j.cell.2007.06.050. PMID: 17719543

Hantschel O*, Wiesner S*, Güttler T, Mackereth CD, Rix LL, Mikes Z, Dehne J, Görlich D, Sattler M, Superti-Furga G. Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl. Mol Cell. 2005 Aug 19;19(4):461-73. doi: 10.1016/j.molcel.2005.06.030. PMID: 16109371

*Equal contribution

Complete List of Publications

see here.


1992 - 1998 Undergraduate studies in Chemistry ("Vordiplom") and Biochemistry ("Diplom"), Free University of Berlin, Germany
1997 - 1998 Erasmus exchange student at the Ecole Nationale Superieure de Chimie, Montpellier, France
1998 Diploma Thesis at Lund University, Sweden
1998 - 2003 Graduate student with Prof. M. Sattler and Prof. M.J. Macias at EMBL Heidelberg, Germany
2003 PhD, Free University of Berlin / EMBL Heidelberg ("summa cum laude")
2003 - 2008 Postdoctoral fellow with Prof. Julie Forman-Kay at the Hospital for Sick Children, University of Toronto, Canada
2008 - 2017 Group Leader at the Max Planck Institute for Developmental Biology, Tübingen, Germany
Since 2017 Group Leader / Lecturer at the University of Regensburg, Germany


Or see here.


Ubiquitin-dependent Cell Signaling


Phone: +49-(0)941-943-7752


E-mail: Silke.Wiesner [at] ur.de