Jentsch.html

Our laboratory has a long-standing interest in proteins of the ubiquitin family. Covalent modification of proteins by attachment of the small protein ubiquitin ("ubiquitylation") mediates a variety of different cellular functions. The best-known function of ubiquitylation is to label proteins for degradation by the proteasome. Other functions include e.g. regulation of protein sorting, gene expression and DNA repair. Eukaryotes also express proteins related to ubiquitin, which can form conjugates with cellular proteins similar to ubiquitin (e.g. SUMO, Rub1, Urm1) or bind proteins non-covalently (Hub1). Our research focuses primarily on the cellular functions of proteins of the ubiquitin family. We identify from yeast and mammalian cells the components of these systems and study their functions in vitro and in vivo. We are increasingly interested in the non-proteolytic functions of ubiquitin family proteins, in particular in DNA repair and pre-mRNA splicing. Moreover, we are interested in chromatin biology, specifically quality control mechanisms and DNA repair pathways.

RESEARCH	PUBLICATIONS	CV
FURTHER READING	AWARDS	LAB MEMBERS
OPEN POSITIONS	MATERIAL REQUESTS	LINKS

RECENT AND CURRENT PROJECTS

	Searching for homology Monitoring homology search during DNA double-strand break repair in vivo. Renkawitz et al., Mol. Cell 50, 261-272, 2013 [PDF] Research Highlights (Nat. Rev. Genet.)		A SUMO-targeted segregase Bergink et al., Nat. Cell Biol., doi:10.1038/ncb2729, 2013 [PDF]
	"SUMO spray" stabilizes protein complexes Protein-group modification and synergy in the SUMO pathway as exemplified in DNA repair. Psakhye and Jentsch, Cell 151, 807-820, 2012 [PDF] Faculty 1000 comments		Call 9-1-1 for repair Noncanonical role of the 9-1-1 clamp in the error-free DNA damage tolerance pathway. Karras et al., Mol. Cell 49, 536-546, 2013 [PDF] Faculty 1000 comments
	A novel mechanism for alternative splicing Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing. Mishra et al., Nature 474, 173-178, 2011 [PDF] Faculty 1000 comments		Timing replication and DNA damage tolerance The RAD6 DNA damage tolerance pathway operates uncoupled from the replication fork and is functional beyond S-phase. Karras and Jentsch, Cell 141, 255-267, 2010 [PDF]
	Meiotic checkpoint control by Red1 Synaptonemal complex formation and meiotic checkpoint signaling are linked to the lateral element protein Red1. Eichinger and Jentsch, PNAS 107, 11370-11375, 2010 [PDF]		Unexpected behavior of broken chromosomes Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. Kalocsay et al., Mol. Cell 33, 335-343, 2009 [PDF]
	A fate switch in the ubiquitin pathway Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation. Siepe and Jentsch, Nat. Cell Biol 11, 967-972, 2009 [PDF]		A molecular Swiss army knife mediates abscission Final stages of cytokinesis and midbody ring formation are controlled by BRUCE. Pohl and Jentsch, Cell 132, 832-845, 2008 [PDF]. Midbody ring disposal by autophagy is a post-abscission event of cytokinesis. Pohl and Jentsch, Nat. Cell Biol 11, 65-70, 2009 [PDF] Faculty 1000 comments

FURTHER READING

Protein group SUMOylation: substrate specificity in the SUMO pathway
Psakhye and Jentsch, Cell 151, 807-820, 2012 Faculty 1000 comments

DNA double-strand break repair by homologous recombination
Renkawitz et al., Mol. Cell 50, 261-272, 2013
Kalocsay et al., Mol. Cell 33, 335-343, 2009

Regulation of the spliceosome by the ubiquitin-like protein Hub1
Mishra et al., Nature 474, 173-178, 2011

Regulation of DNA damage tolerance and repair by ubiquitin and SUMO: The PCNA switch
        Karras et al., Mol. Cell 49, 536-546, 2013
        Karras and Jentsch, Cell 141, 255-267, 2010
        Parnas et al., EMBO J. 29, 2611-2622
        Arakawa et al., PLOS Biol. 4, 1947-1956, 2006
        Pfander et al., Nature 436, 428-433, 2005
        Hoege et al., Nature 419, 135-141, 2002
        Ulrich and Jentsch, EMBO J.19, 3388-3397, 2000

SnapShot:The SUMO pathway. Creton and Jentsch, Cell 143, 2010

Review: Principles of ubiquitin and SUMO modifications in DNA repair. Bergink and Jentsch, Nature 458, 461-467, 2009

Review: PCNA, the maestro of the replication fork. Moldovan et al., Cell 129, 665-679, 2007

Regulation of homologous recombination by ubiquitin and SUMO
       Bergink et al., Nat. Cell Biol., doi:10.1038/ncb2729, 2013
       Torres-Rosell et al., Nat. Cell Biol. 9, 923-931, 2007
       Sacher et al., Nat. Cell Biol. 8, 1284-1290, 2006

Regulation of sister chromatid cohesion: Eco1 and SUMO
Moldovan et al., Mol Cell 23, 723-732, 2006

Proteasome-mediated protein processing: the OLE pathway
        Piwko and Jentsch, Nat. Struct. Mol. Biol. 13, 691-697, 2006
        Rape et al., Cell 107, 667-677, 2001
        Hoppe et al., Cell 102, 577-586, 2000

Substrate delivery to the proteasome: the escort pathway
        Richly et al., Cell 120, 73-84, 2005
        Koegl et al., Cell 96, 635-644, 1999

Review: Pin1, a novel switch in the ubiquitin pathway. Cell Cycle 8, 3800-3801.

The ubiquitin/SUMO-selective chaperone (segregase) Cdc48 and its co-factors
        Bergink et al., Nat. Cell Biol., doi:10.1038/ncb2729, 2013
        Rumpf and Jentsch, Mol. Cell 21, 261-269, 2006
        Richly et al., Cell 120, 73-84, 2005
        Braun et al., EMBO J. 21, 615-621, 2002
        Rape et al., Cell 107, 667-677, 2001

Review: Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Jentsch & Rumpf, TIBS 32, 6-11, 2006

ER-associated degradation, ERAD
        Braun and Jentsch, EMBO Rep. 8, 1176-1182, 2007
        Braun et al., EMBO J. 21, 615-621, 2002
        Mayer et al., EMBO J., 17, 3251-3257, 1998

Regulation of apoptosis and cytokinesis by BRUCE, a giant E2/E3 ubiquitin ligase
        Pohl and Jentsch, Nat. Cell Biol 11, 65-70, 2009
        Pohl, C. and Jentsch, S. Cell 132, 832-845, 2008
        Bartke et al., Mol. Cell, 14, 801-811, 2004
        Lotz et al., Mol. Cell. Biol. 24, 9339-9350, 2004
        Hauser et al., J. Cell Biol. 141, 1415-1422, 1998

        Movie: Ubiquitin during cytokinesis
        Movie: Midbody ring during cytokinesis

CURRENT POSITION	Director	Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried/München, Germany
2011	Managing Director	Max Planck Institute of Biochemistry, Martinsried/München, Germany
2010-2012	Member of the Managing Board of Directors	Max Planck Institute of Biochemistry, Martinsried/München, Germany
2003	Managing Director	Max Planck Institute of Biochemistry, Martinsried/München, Germany
2001-2004	Member of the Managing Board of Directors	Max Planck Institute of Biochemistry, Martinsried/München, Germany
since 2006	Honorary Professor (Prof. h.c.)	Fudan University, Shanghai, China
since 2001	Honorary Professor	Ludwig Maximilians University, München, Germany
since 1998	Director	Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried/München, Germany
1996-1998	Deputy Director	ZMBH, Center of Molecular Biology, Heidelberg University, Germany
1993-1998	Professor of Cell Biology	ZMBH, Center of Molecular Biology, Heidelberg University, Germany
1988-1993	Junior Group Leader	Friedrich Miescher Laboratory of the Max Planck Society, Tübingen, Germany
1985-1988	Postdoctoral Fellow/Associate	Department of Biology, Massachusetts Institute of Technology, Cambridge MA, USA Laboratory of Alexander Varshavsky
1983-1985	Research Assistant	Max Planck Institute of Molecular Genetics, Berlin, Germany Laboratory of Thomas A. Trautner
1979-1983	Graduate Student	Max Planck Institute of Molecular Genetics, Berlin, Germany Laboratory of Thomas A. Trautner
1979	Diploma Student	Max Planck Institute of Molecular Genetics, Berlin, Germany Laboratory of Thomas A. Trautner
1975-1979	Student of Biology	Free University Berlin, Germany