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Stefan Jentsch
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. For more details visit: http://www.biochem.mpg.de/jentsch/Jentsch.htm l
Role in RUBICON:
Coordinator for WP "Functions"
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| RELATED NEWS (2/2) |
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C2a: 2009, September 22-26, RUBICON and EMBO Conference: Ubiquitin and Ubiquitin-like Modifiers in Health and Disease, Riva del Garda, Italy

PR04 - 09.02.13: How cells handle broken chromosomes

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258_DE_jentsch-publications

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Thomas Sommer (Principal Investigator / Thomas Sommer's Group)
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