Stefan Jentsch

Summary

Country: Germany

Publications

  1. ncbi request reprint RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    Carsten Hoege
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
    Nature 419:135-41. 2002
  2. doi request reprint Control of nuclear activities by substrate-selective and protein-group SUMOylation
    Stefan Jentsch
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany email
    Annu Rev Genet 47:167-86. 2013
  3. ncbi request reprint Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?
    Stefan Jentsch
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Trends Biochem Sci 32:6-11. 2007
  4. doi request reprint Regulatory Functions of Ubiquitin and SUMO in DNA Repair Pathways
    Stefan Jentsch
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152, Martinsried, Germany
    Subcell Biochem 54:184-94. 2010
  5. doi request reprint Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction
    Steven Bergink
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Nat Cell Biol 15:526-32. 2013
  6. ncbi request reprint SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    Boris Pfander
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 436:428-33. 2005
  7. doi request reprint Noncanonical role of the 9-1-1 clamp in the error-free DNA damage tolerance pathway
    Georgios Ioannis Karras
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 49:536-46. 2013
  8. doi request reprint The RAD6 DNA damage tolerance pathway operates uncoupled from the replication fork and is functional beyond S phase
    Georgios I Karras
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 141:255-67. 2010
  9. ncbi request reprint Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    Sebastian Rumpf
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 21:261-9. 2006
  10. ncbi request reprint Control of Rad52 recombination activity by double-strand break-induced SUMO modification
    Meik Sacher
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nat Cell Biol 8:1284-90. 2006

Collaborators

Detail Information

Publications38

  1. ncbi request reprint RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    Carsten Hoege
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
    Nature 419:135-41. 2002
    ..We demonstrate that these modifications differentially affect resistance to DNA damage, and that damage-induced PCNA ubiquitination is elementary for DNA repair and occurs at the same conserved residue in yeast and humans...
  2. doi request reprint Control of nuclear activities by substrate-selective and protein-group SUMOylation
    Stefan Jentsch
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany email
    Annu Rev Genet 47:167-86. 2013
    ..We propose that collective SUMOylation is typical for nuclear assemblies and argue that SUMO serves as a distinguishing mark for functionally engaged protein fractions. ..
  3. ncbi request reprint Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?
    Stefan Jentsch
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Trends Biochem Sci 32:6-11. 2007
    ..We discuss how Cdc48 might use this 'gearbox activity' to control protein fate and propose a similar mode of action for the 19S cap of the proteasome...
  4. doi request reprint Regulatory Functions of Ubiquitin and SUMO in DNA Repair Pathways
    Stefan Jentsch
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D 82152, Martinsried, Germany
    Subcell Biochem 54:184-94. 2010
    ..In this chapter we will illustrate some key functions of ubiquitin and SUMO in the control of selected DNA repair pathways...
  5. doi request reprint Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction
    Steven Bergink
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Nat Cell Biol 15:526-32. 2013
    ..We propose that Cdc48, through its ability to associate with co-factors that have affinities for ubiquitin and SUMO, connects the two modification pathways for protein degradation or other regulatory purposes...
  6. ncbi request reprint SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    Boris Pfander
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 436:428-33. 2005
    ..Our finding suggests a model in which SUMO-modified PCNA recruits Srs2 in S phase in order to prevent unwanted recombination events of replicating chromosomes...
  7. doi request reprint Noncanonical role of the 9-1-1 clamp in the error-free DNA damage tolerance pathway
    Georgios Ioannis Karras
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 49:536-46. 2013
    ..Our findings thus reveal unexpected cooperation in the error-free pathway between the two related clamps and indicate that 9-1-1 plays a broader role in the DNA damage response than previously assumed...
  8. doi request reprint The RAD6 DNA damage tolerance pathway operates uncoupled from the replication fork and is functional beyond S phase
    Georgios I Karras
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 141:255-67. 2010
    ..We therefore propose that the RAD6 pathway acts on single-stranded gaps left behind newly restarted replication forks...
  9. ncbi request reprint Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    Sebastian Rumpf
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 21:261-9. 2006
    ..We propose that the balance between the distinct substrate-processing cofactors may determine whether a substrate is multiubiquitylated and routed to the proteasome for degradation or deubiquitylated and/or released for other purposes...
  10. ncbi request reprint Control of Rad52 recombination activity by double-strand break-induced SUMO modification
    Meik Sacher
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nat Cell Biol 8:1284-90. 2006
    ..Furthermore, our data indicate that sumoylation becomes particularly relevant for those Rad52 molecules that are engaged in recombination...
  11. ncbi request reprint A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    Holger Richly
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 120:73-84. 2005
    ..In yeast, this escort pathway guides a transcription factor from its activation in the cytosol to its final degradation and also mediates proteolysis at the endoplasmic reticulum by the ERAD pathway...
  12. ncbi request reprint Prolyl isomerase Pin1 acts as a switch to control the degree of substrate ubiquitylation
    Dirk Siepe
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nat Cell Biol 11:967-72. 2009
    ..This suggests that the Pin1 activity is often translated into a fate-determining ubiquitylation switch, and that Pin1 may affect the degree of substrate ubiquitylation in other pathways as well...
  13. ncbi request reprint PCNA controls establishment of sister chromatid cohesion during S phase
    George Lucian Moldovan
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 23:723-32. 2006
    ..Our study thus indicates that PCNA, a central matchmaker for replication-linked functions, is also crucially involved in the establishment of cohesion in S phase...
  14. pmc Synaptonemal complex formation and meiotic checkpoint signaling are linked to the lateral element protein Red1
    Christian S Eichinger
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Proc Natl Acad Sci U S A 107:11370-5. 2010
    ..Thus, Red1, in addition to its structural role in the SC, is a crucial coordinator of meiosis by coupling checkpoint signaling to SC formation...
  15. pmc SM-protein-controlled ER-associated degradation discriminates between different SNAREs
    Sigurd Braun
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, Munich D 82152, Germany
    EMBO Rep 8:1176-82. 2007
    ..Thus, our findings identify Sly1 as a discriminating regulator of SNARE levels and indicate that Sly1-controlled ERAD might regulate the balance between different Qa-SNARE proteins...
  16. ncbi request reprint PCNA, the maestro of the replication fork
    George Lucian Moldovan
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18 82152 Martinsried, Germany
    Cell 129:665-79. 2007
    ..Switching of PCNA partners may be triggered by affinity-driven competition, phosphorylation, proteolysis, and modification of PCNA by ubiquitin and SUMO...
  17. pmc Role of the ubiquitin-like protein Hub1 in splice-site usage and alternative splicing
    Shravan Kumar Mishra
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 474:173-8. 2011
    ..Our study indicates a novel mechanism for splice site utilization that is guided by non-covalent modification of the spliceosome by an unconventional ubiquitin-like modifier...
  18. doi request reprint Monitoring homology search during DNA double-strand break repair in vivo
    Jörg Renkawitz
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany
    Mol Cell 50:261-72. 2013
    ..Our study thus reveals crucial parameters for homology search in vivo and emphasizes the importance of linear distance, chromosome architecture, and proximity for recombination efficiency...
  19. ncbi request reprint Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    Wojciech Piwko
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nat Struct Mol Biol 13:691-7. 2006
    ..Furthermore, we provide evidence that the ability of the proteasome to initiate proteolysis from an internal site and to proceed via bidirectional polypeptide degradation may be relevant for the complete degradation of proteins as well...
  20. ncbi request reprint Taking a bite: proteasomal protein processing
    Michael Rape
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, 82152 Martinsried, Germany
    Nat Cell Biol 4:E113-6. 2002
    ..How distinct protein domains are spared from degradation remains a matter of debate. Here, we discuss several models and suggest a novel mechanism for proteasomal processing...
  21. ncbi request reprint Mechanisms and principles of homology search during recombination
    Jörg Renkawitz
    1 Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany 2 Institute of Science and Technology IST Austria, 3400 Klosterneuburg, Austria 3
    Nat Rev Mol Cell Biol 15:369-83. 2014
    ..They also aid our understanding of how homology search might lead to unwanted and potentially disease-promoting recombination events. ..
  22. doi request reprint Midbody ring disposal by autophagy is a post-abscission event of cytokinesis
    Christian Pohl
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nat Cell Biol 11:65-70. 2009
    ..Thus our findings suggest that autophagy has a broader role than previously assumed, and that cell renovation by clearing from superfluous large macromolecular assemblies, such as MRs, is an important autophagic function...
  23. ncbi request reprint Identification of SUMO-protein conjugates
    Meik Sacher
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany
    Methods Enzymol 399:392-404. 2005
    ..Here we discuss procedures that can circumvent identification problems and describe methods for their verification...
  24. pmc BRUCE, a giant E2/E3 ubiquitin ligase and inhibitor of apoptosis protein of the trans-Golgi network, is required for normal placenta development and mouse survival
    Kristina Lotz
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell Biol 24:9339-50. 2004
    ..Thus, although BRUCE is broadly expressed in embryonic, extraembryonic, and adult mouse tissues, this bifunctional protein might play a unique role in normal trophoblast differentiation and embryonic survival...
  25. doi request reprint Final stages of cytokinesis and midbody ring formation are controlled by BRUCE
    Christian Pohl
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 132:832-45. 2008
    ..We propose that BRUCE coordinates multiple steps required for abscission and that ubiquitylation may be a crucial trigger...
  26. doi request reprint Principles of ubiquitin and SUMO modifications in DNA repair
    Steven Bergink
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Nature 458:461-7. 2009
    ....
  27. doi request reprint Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break
    Marian Kalocsay
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 33:335-43. 2009
    ..Thus, a persistent DSB induces a multifaceted response, which is linked to a specific chromatin mark...
  28. pmc The ubiquitin-like protein HUB1 forms SDS-resistant complexes with cellular proteins in the absence of ATP
    Jens Lüders
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    EMBO Rep 4:1169-74. 2003
    ..We propose that HUB1 may act as a novel protein modulator through the formation of tight, possibly noncovalent interactions with target proteins...
  29. doi request reprint Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    Ivan Psakhye
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Cell 151:807-20. 2012
    ..We propose that SUMOylation may thus often target a protein group rather than individual proteins, whereas localized modification enzymes and highly specific triggers ensure specificity...
  30. ncbi request reprint Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase
    Till Bartke
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Mol Cell 14:801-11. 2004
    ..Our work suggests that, owing to its two activities and its localization, BRUCE may function as a specialized regulator of cell death pathways...
  31. ncbi request reprint Productive RUPture: activation of transcription factors by proteasomal processing
    Michael Rape
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
    Biochim Biophys Acta 1695:209-13. 2004
    ..Examples are proteins of the mammalian NF-kappaB family and the yeast proteins SPT23 and MGA2. In this review, we summarize the available data and suggest a mechanistic model for proteasomal processing...
  32. pmc Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates
    Sigurd Braun
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D 82152 Martinsried, Germany
    EMBO J 21:615-21. 2002
    ..We propose that CDC48(UFD1/NPL4) functions as a segregase that liberates ubiquitylated proteins from non-modified partners...
  33. ncbi request reprint Deadly encounter: ubiquitin meets apoptosis
    Veronika Jesenberger
    Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18 A, 82152 Martinsried, Germany
    Nat Rev Mol Cell Biol 3:112-21. 2002
    ..Moreover, key regulators of apoptosis themselves seem to have an active part in the proteolytic inactivation of death executors...
  34. ncbi request reprint Varshavsky's contributions
    Wolfgang Baumeister
    Science 306:1290-2. 2004
  35. pmc A role for PCNA ubiquitination in immunoglobulin hypermutation
    Hiroshi Arakawa
    Gesellschaft für Strahlen Forschung, Institute for Molecular Radiobiology, Neuherberg Munich, Germany
    PLoS Biol 4:e366. 2006
    ..This is the first evidence, to our knowledge, that vertebrates exploit the PCNA-ubiquitin pathway for immunoglobulin hypermutation, most likely through the recruitment of error-prone DNA polymerases...
  36. ncbi request reprint The Smc5-Smc6 complex and SUMO modification of Rad52 regulates recombinational repair at the ribosomal gene locus
    Jordi Torres-Rosell
    Cell Cycle Group, MRC Clinical Sciences Centre, Imperial College London, Du Cane Road, London W12 0NN, UK
    Nat Cell Biol 9:923-31. 2007
    ..Our study also suggests a key role of sumoylation for nucleolar dynamics, perhaps in the compartmentalization of nuclear activities...