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Am Klopferspitz 18
82152 Martinsried/Munich
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The Max Planck Institute of Biochemistry offers outstanding research and training opportunities and has an exceptional strength at molecular, cell, and structural biology. The institute's international graduate program with special seminar series, courses, scientific retreats, and its international atmosphere makes the institute distinctively attractive for graduate students and postdocs.
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General description: Our laboratory has a long-standing interest in protein modification by ubiquitin and ubiquitin-like proteins. Our research focuses primarily on functional aspects. We identify from yeast and mammalian cells the enzymatic components of these systems, clone the corresponding genes, and study their functions in vitro and in vivo. We showed by genetic analysis that enzymes of the ubiquitin pathway mediate degradation of abnormal proteins, stress tolerance, DNA repair, and cell cycle progression. We discovered that ubiquitylated proteins are degraded by the proteasome in vivo and found that ER-associated protein degradation (ERAD) involves the cytosolic ubiquitin/proteasome system. We also discovered the highly conserved ubiquitin-like modifier Rub1 (NEDD8) and described its complete conjugation system. More recently, we became particularly interested in the non-proteolytic functions of ubiquitylation and in the function of the ubiquitin-like modifier SUMO.
Role in RUBICON: The group will study the role of ubiquitin and SUMO in DNA transactions (DNA replication, recombination, repair). Recently, we found that PCNA is ubiquitylated and SUMOylated, and that these modifications regulate specific replication-linked functions like DNA repair, recombination, and sister chromatid cohesion (Hoege et al., Nature 419, 135-141, 2002; Pfander et al., Nature 436, 428-433, 2005; Moldovan et al., Mol. Cell 23, 723-732, 2006). The goal of the future work is to find out how ubiquitin and SUMO mediate descision making at the replication fork.
For further information please visit our detailed web site (http://www.biochem.mpg.de/jentsch/Jentsch.htm l)
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PCNA modified by ubiquitin (see: Hoege et al., Nature 419, 135-141, 2002; Pfander et al., Nature 436, 428-433, 2005)
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| MEMBERS (18/18) |
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Stefan Mueller, Research Associate (Group Leader / Stefan Jentsch's Group)

Steven Bergink, Post-doc (Stefan Jentsch's Group)

Sandrine Creton, Post-doc (Stefan Jentsch's Group)

Gang Qin, Post-doc (Stefan Jentsch's Group)

Shravan Mishra, Post-doc (Stefan Jentsch's Group)

Tim Ammon, Ph.D. Student (Stefan Jentsch's Group)

Giorgios Karras, Post-doc (Stefan Jentsch's Group)

Kenji Schorpp, Post-doc (Stefan Jentsch's Group)

Michael Schwarz, Ph.D. Student (Stefan Jentsch's Group)

Ivan Psakhye, Ph.D. Student (Stefan Jentsch's Group)

Maximilian Kern, Ph.D. Student (Stefan Jentsch's Group)

Elisabeth Finkbeiner, Ph.D. Student (Stefan Jentsch's Group)

Rebecca Ullmann, Ph.D. Student (Stefan Jentsch's Group)

Sean Lin, Ph.D. Student (Stefan Jentsch's Group)

Florian Paasch, Ph.D. Student (Stefan Jentsch's Group)

Joerg Renkawitz, Ph.D. Student (Stefan Jentsch's Group)

Julian Stingele, Ph.D. Student (Stefan Jentsch's Group)
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