Contact Information: Secretary
Contact Information: Secretary
Klara Schwander
Phone:+49 89 8578 3000Fax:+49 89 8578 3011

Postal Address, Max Planck Institute of Biochemistry, Dept. of Molecular Cell Biology, Am Klopferspitz 18, 82152, Martinsried (Munich), Germany


A new cellular garbage control pathway with relevance for neurodegenerative diseases
Several human neurodegenerative diseases are linked to an accumulation of abnormal and aggregated proteins in cells. Cellular “garbage” of this type can be removed from cells by sweeping them via a “self-eating” pathway (autophagy) to a cellular recycling station known as the lysosome. The newly identified adaptors, termed CUET proteins, recognize labeled cellular protein waste and guide them efficiently to the lysosome for destruction. 

Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family.
Lu, K., Psakhye, I., and Jentsch, S.
Cell 158, 549-563, 2014.
Press release
Feature in SGD
F1000 comments
Comment by Orban & Klionsky

Discovery of a new DNA repair pathway
Reagents like formaldehyde, produced by cells e.g. upon histone de-methylation, or taken up from the environment, can cause highly toxic, cancerogenous DNA-protein crosslinks, which interfere with replication. The newly identified DNA repair pathway destroys the protein components of DNA-protein crosslinks, thereby enabling cells to duplicate their genome. 

A DNA-dependent protease involved in DNA-protein crosslink repair.
Stingele et al., 
Cell 158, 327-338, 2014
Press Release
F1000 comments


DNA-protein crosslink repair
Stingele and Jentsch
Nat. Rev. Mol. Cell Biol. 16, 455-460, 2015

DNA-protein crosslink repair: proteases as DNA repair enzymes
Stingele, Habermann and Jentsch
Trends Biochem. Sci. 40, 67-71, 2015

Mechanisms and principles of homology search during recombination
Renkawitz, Lademann and Jentsch
Nat. Rev. Mol. Cell Biol15, 369-383, 2014

Control of nuclear activities by substrate-selective and protein group modification
Psakhye and Jentsch
Ann. Rev. Genet. 47, 185-204, 2014

ERC Advanced Grant
Our laboratory receives 2.48 million Euros in EU funding

Department of Molecular Cell Biology

Header image 1372859705

Ubiquitin Family Proteins, DNA Transactions, Chromatin Biology, Autophagy

Our laboratory has a long-standing interest in proteins of the ubiquitin family. Covalent modification of proteins by attachment of ubiquitin (ubiquitylation) is best known for its function to label proteins for degradation by the proteasome. However, ubiquitylation plays non-proteolytic roles as well, e.g. for DNA repair, protein sorting, gene expression and signal transduction. Other members of the ubiquitin family, e.g. SUMO, Rub1(NEDD8), Urm1, Hub1, and Atg8, regulate the ubiquitin pathway, affect protein-protein interactions, control DNA repair, transcription, pre-mRNA splicing, or mediate autophagy. 

We are conducting basic research with a focus on functional aspects related to ubiquitin family proteins. We identify the components of these systems and study their roles in vitro and in vivo. We are particularly interested in the non-proteolitic (non-proteasomal) functions of ubiquitin family proteins and currently focus primarily on their roles in DNA repair, pre-mRNA splicing and autophagy. Moreover, we have a general interest in DNA repair, genome stability and chromatin biology - in particular if ubiquitin family proteins are involved. For the "discovery phase" we primarily use the genetically tractable budding yeast (Saccharomyces cerevisiae) as a model system. However, to extend the significance of our findings made in yeast to a more universal level, we complement our studies by analyzing the respective functions also in mammalian cells. [Header illustration: structures of ubiquitin, Rub1, SUMO, Hub1]

Examples of our work with the respective papers are found here.



STEFAN JENTSCH - Director and Group Leader

PhD 1983 Max Planck Institute of Molecular Genetics,
     Berlin, Germany (Free University Berlin)
Postdoctoral work at Massachusetts Institute of Technology (MIT),
     Cambridge, USA
Max Planck Research Group Leader at Friedrich Miescher Laboratory
     of the Max Planck Society, Tuebingen, Germany
Professor at Center for Molecular Biology (ZMBH),
     Heidelberg University, Germany
Director at MPI of Biochemistry and Member of the Max Planck Society since 1998

At the Max Planck Institute of Biochemistry since 1998

ERC Advanced Grant (2013)
Louis-Jeantet Prize for Medicine (2011)
Max-Planck Research Award (2003)
Otto Bayer Award (1996)
Gottfried Wilhelm Leibniz Prize (1993)
Otto Klung Prize for Chemistry (1992)

Elected member of EMBO, German Academy of Sciences Leopoldina & Academia Europaea; elected AAAS Fellow; honorary professor at Fudan University, Shanghai, China



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