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Groupleader: Sebastian Schuck
Sebastian Schuck
Organelle Homeostasis
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Research
Organelle Homeostasis
Biogenesis and Degradation of the Endoplasmic Reticulum
Eukaryotic cells show striking differences in the abundance and architecture of their organelles. Moreover, cells rapidly adjust the size and shape of their organelles to changing physiological demands. This remarkable capacity for adaptation enables cells to maintain homeostasis during differentiation, stress and disease. The underlying molecular mechanisms are fundamental for proper cell function and uncovering them is a fascinating challenge.
We want to elucidate how cells ensure homeostasis of the endoplasmic reticulum (ER). We are asking questions such as: How do cells shape their ER? How do they know how much ER they need? How do they adjust ER size and function to physiological demand? How do they recognize damaged ER components and eliminate them? To answer these questions, we investigate three related processes: (1) ER membrane biogenesis, which enables organelle expansion and remodeling, (2) ER-phagy, which mediates autophagic organelle degradation, and (3) SHRED, which regulates proteasomal degradation of misfolded cytosolic and ER membrane proteins. We explore these processes in budding yeast but also in mammalian cells.
We want to elucidate how cells ensure homeostasis of the endoplasmic reticulum (ER). We are asking questions such as: How do cells shape their ER? How do they know how much ER they need? How do they adjust ER size and function to physiological demand? How do they recognize damaged ER components and eliminate them? To answer these questions, we investigate three related processes: (1) ER membrane biogenesis, which enables organelle expansion and remodeling, (2) ER-phagy, which mediates autophagic organelle degradation, and (3) SHRED, which regulates proteasomal degradation of misfolded cytosolic and ER membrane proteins. We explore these processes in budding yeast but also in mammalian cells.
ER membrane biogenesis
The ER is a morphologically complex organelle with vital functions in protein folding and lipid synthesis. When the ER is unable to fold its load of newly synthesized polypeptides, misfolded proteins accumulate and cause ER stress. Misfolded proteins activate the unfolded protein response (UPR), which increases the protein folding capacity of the ER and induces ER-associated degradation. In this way, the UPR promotes the removal of misfolded proteins. Related mechanisms cooperate with the UPR to clear troublesome proteins, including proteasome biogenesis (Schmidt et al, 2019). Furthermore, the UPR triggers massive expansion of the ER membrane by activating lipid synthesis (Figure 1; Schuck et al, 2009). We have identified genes required for ER expansion and determined how they regulate lipid metabolism and ER membrane biogenesis (Papagiannidis, Bircham et al, 2021). Secretory cells, such as antibody-secreting plasma cells, need to expand the ER membrane during differentiation. Therefore, finding out how cells adjust ER size will help us understand how cells respond to stress and also how they differentiate.
Figure 1. ER membrane expansion. Yeast expressing Sec63-GFP to highlight the cytoplasmic ER (cER) and the nuclear envelope (NE). Yeast exposed to ER stress have a vastly expanded cytoplasmic ER.
Autophagy (cellular self-eating) is another response to ER stress. Upon stress, cells turn on selective autophagy of the ER, which can occur by macroautophagy and microautophagy (Schuck, 2020). Our focus is micro-ER-phagy, which in yeast involves a spectacular restructuring of ER that gives rise multilamellar whorls. These whorls are then sent to the lysosome for degradation (Figure 2; Schuck et al., 2014). We have shown that micro-ER-phagy does not require the well-known core autophagy machinery but depends on ESCRT proteins (Schäfer et al., 2020). Nonetheless, our understanding of micro-ER-phagy is still, well, a litte crude. Through micro-ER-phagy, cells may sacrifice parts of their ER to destroy protein aggregates and damaged organelle membrane. Moreover, when stress has been resolved, micro-ER-phagy may downsize the ER and reverse organelle expansion. In this way, the UPR and ER-phagy may work together to refold or degrade damaged proteins and to expand or shrink the ER as needed. Hence, ER-phagy helps maintain ER homeostasis and may be relevant for diseases impinging on ER function, such as cancer and diabetes. We are keen to learn more about the molecular events during autophagy of ER whorls and to define the physiological roles of micro-ER-phagy in both yeast and mammals.
Figure 2. Correlative light and electron microscopy of micro-ER-phagy. Micro-ER-phagy can be triggered by expression of the 'ER-phagy inducer', an artificial GFP-tagged transmembrane protein. Fluorescence images show a ring-shaped structure positive for a general ER marker and the ER-phagy inducer. The corresponding electron micrograph reveals that this structure is a large multilamellar ER whorl inside the yeast lysosome.
SHRED
Protein folding is error-prone, especially during stress. Cells possess elaborate quality control machinery, including numerous chaperones and ubiquitin ligases, to promote proper folding and degrade folding failures. Stress responses like the UPR tune quality control to current demand. We have uncovered a novel stress response pathway termed SHRED, for stress-induced homeostatically regulated protein degradation (Figure 3; Szoradi et al., 2018). SHRED is activated when stress stimulates transcription of the Roq1 gene. The Roq1 protein is cleaved by the protease Ynm3. Truncated Roq1∆21 binds to the ubiquitin ligase Ubr1 as a pseudosubstrate, reprograms Ubr1's substrate specificity and directs it towards misfolded cytosolic and ER membrane proteins. The resulting more stringent quality control enhances stress resistance. Deteriorating protein quality control during aging is a key factor for the onset of neurodegenerative diseases such as Alzheimer’s. Moreover, cancer cells suffer from chronic folding stress and depend on heightened quality control for survival. A deeper understanding of how quality control is regulated may therefore inspire new therapeutic approaches.
Figure 3. SHRED. Under non-stress conditions, the ubiquitin ligase Ubr1 degrades proteins with positively charged N-terminal residues as part of the N-degron pathway (left). Under stress conditions, Roq1 is produced, is cleaved by Ynm3 and binds to Ubr1 as a pseudosubstrate. This reprograms Ubr1 and stimulates the degradation of misfolded proteins (right).
Selected publications
Papagiannidis D*, Bircham PW*, Lüchterborg C, Pajonk O, Ruffini G, Brügger B, Schuck S (2021) Ice2 promotes ER membrane biogenesis in yeast by inhibiting the conserved lipin phosphatase complex. EMBO Journal. (abstract)
Schuck S (2020) Microautophagy - distinct molecular mechanisms handle cargoes of many sizes. Journal of Cell Science. (abstract)
Schäfer JA, Schessner JP, Bircham PW, Tsuji T, Funaya C, Pajonk O, Schaeff K, Ruffini G, Papagiannidis D, Knop M, Fujimoto T, Schuck S (2020) ESCRT machinery mediates selective microautophagy of endoplasmic reticulum in yeast. EMBO Journal. (abstract)
Schmidt RM, Schessner JP, Borner GH, Schuck S (2019) The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance. eLife. (abstract)
Szoradi T, Schaeff K, Garcia-Rivera EM, Itzhak DN, Schmidt RM, Bircham PW, Leiss K, Diaz-Miyar J, Chen VK, Muzzey D, Borner GH, Schuck S (2018) SHRED is a regulatory cascade that reprograms Ubr1 substrate specificity for enhanced protein quality control during stress. Molecular Cell. (abstract)
Schuck S, Gallagher CM, Walter P (2014) ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery. Journal of Cell Science. (abstract)
Schuck S, Prinz WA, Thorn KS, Voss C, Walter P (2009) Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. Journal of Cell Biology. (abstract)
Schuck S, Prinz WA, Thorn KS, Voss C, Walter P (2009) Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. Journal of Cell Biology. (abstract)
Publications
Research articles
Papagiannidis D*, Bircham PW*, Lüchterborg C, Pajonk O, Ruffini G, Brügger B, Schuck S (2021) Ice2 promotes ER membrane biogenesis in yeast by inhibiting the conserved lipin phosphatase complex. EMBO Journal. (abstract)
Schäfer JA, Schessner JP, Bircham PW, Tsuji T, Funaya C, Pajonk O, Schaeff K, Ruffini G, Papagiannidis D, Knop M, Fujimoto T, Schuck S (2020) ESCRT machinery mediates selective microautophagy of endoplasmic reticulum in yeast. EMBO Journal. (abstract)
Schmidt RM, Schessner JP, Borner GH, Schuck S (2019) The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance. eLife. (abstract)
Szoradi T, Schaeff K, Garcia-Rivera EM, Itzhak DN, Schmidt RM, Bircham PW, Leiss K, Diaz-Miyar J, Chen VK, Muzzey D, Borner GH, Schuck S (2018) SHRED is a regulatory cascade that reprograms Ubr1 substrate specificity for enhanced protein quality control during stress. Molecular Cell. (abstract)
Schäfer JA, Schessner JP, Bircham PW, Tsuji T, Funaya C, Pajonk O, Schaeff K, Ruffini G, Papagiannidis D, Knop M, Fujimoto T, Schuck S (2020) ESCRT machinery mediates selective microautophagy of endoplasmic reticulum in yeast. EMBO Journal. (abstract)
Schmidt RM, Schessner JP, Borner GH, Schuck S (2019) The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance. eLife. (abstract)
Szoradi T, Schaeff K, Garcia-Rivera EM, Itzhak DN, Schmidt RM, Bircham PW, Leiss K, Diaz-Miyar J, Chen VK, Muzzey D, Borner GH, Schuck S (2018) SHRED is a regulatory cascade that reprograms Ubr1 substrate specificity for enhanced protein quality control during stress. Molecular Cell. (abstract)
Schuck S, Gallagher CM, Walter P (2014) ER-phagy mediates selective degradation of endoplasmic reticulum independently of the core autophagy machinery. Journal of Cell Science. (abstract)
Kannegaard E, Rego EH, Schuck S, Feldman JL, Marshall WF (2014) Quantitative analysis and modeling of katanin function in flagellar length control. Molecular Biology of the Cell. (abstract)
Moreira KE*, Schuck S*, Schrul B, Fröhlich F, Moseley JB, Walther TC, Walter P (2012) Seg1 controls eisosome assembly and shape. Journal of Cell Biology. (abstract)
Castillo K, Rojas-Rivera D, Lisbona F, Caballero B, Nassif M, Court FA, Schuck S, Ibar C, Walter P, Sierralta, J, Glavic A, Hetz C (2011) BAX inhibitor-1 regulates autophagy by controlling the IRE1α branch of the unfolded protein response. EMBO Journal. (abstract)
Rubio C, Pincus D, Korennykh A, Schuck S, El-Samad H, Walter P (2011) Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity. Journal of Cell Biology. (abstract)
Wolf J, Reimer T, Schuck S, Rüder C, Gerlach K, Müller EC, Otto A, Dörken B, Rehm A (2010) Role of EBAG9 protein in coat protein complex I-dependent glycoprotein maturation and secretion processes in tumor cells. FASEB Journal. (abstract)
Schuck S, Prinz WA, Thorn KS, Voss C, Walter P (2009) Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. Journal of Cell Biology. (abstract)
Lingwood D, Schuck S, Ferguson C, Gerl MJ, Simons K (2009). Generation of cubic membranes by controlled homotypic interaction of membrane proteins in the endoplasmic reticulum. Journal of Biological Chemistry. (abstract)
Torkko JM, Manninen A, Schuck S, Simons K (2008). Depletion of apical transport proteins perturbs epithelial cyst formation and ciliogenesis. Journal of Cell Science. (abstract)
Schuck S*, Gerl MJ*, Ang AL, Manninen A, Keller P, Mellman I, Simons K (2007) Rab10 is involved in basolateral transport in polarized MDCK cells. Traffic. (abstract)
Schuck S*, Manninen A*, Honsho M, Füllekrug J, Simons K (2004) Generation of single and double knockdowns in polarized epithelial cells by retrovirus-mediated RNA interference. Proceedings of the National Academy of Sciences USA. (abstract)
Schuck S*, Honsho M*, Ekroos K, Shevchenko A, Simons K (2003) Resistance of cell membranes to different detergents. Proceedings of the National Academy of Sciences USA. (abstract)
Schuck S, Soloaga A, Schratt G, Arthur JS, Nordheim A (2003) The kinase MSK1 is required for induction of c-fos by lysophosphatidic acid in mouse embryonic stem cells. BMC Molecular Biology (abstract)
Schratt G, Weinhold B, Lundberg A, Schuck S, Berger J, Schwarz H, Weinberg R, Ruther U, Nordheim A (2001) Serum response factor is required for immediate-early gene activation yet is dispensable for proliferation of embryonic stem cells. Molecular and Cellular Biology. (abstract)
Reviews, commentaries and book chapters
Schuck S (2020) Microautophagy - distinct molecular mechanisms handle cargoes of many sizes. Journal of Cell Science. Review (abstract)
Kannegaard E, Rego EH, Schuck S, Feldman JL, Marshall WF (2014) Quantitative analysis and modeling of katanin function in flagellar length control. Molecular Biology of the Cell. (abstract)
Moreira KE*, Schuck S*, Schrul B, Fröhlich F, Moseley JB, Walther TC, Walter P (2012) Seg1 controls eisosome assembly and shape. Journal of Cell Biology. (abstract)
Castillo K, Rojas-Rivera D, Lisbona F, Caballero B, Nassif M, Court FA, Schuck S, Ibar C, Walter P, Sierralta, J, Glavic A, Hetz C (2011) BAX inhibitor-1 regulates autophagy by controlling the IRE1α branch of the unfolded protein response. EMBO Journal. (abstract)
Rubio C, Pincus D, Korennykh A, Schuck S, El-Samad H, Walter P (2011) Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity. Journal of Cell Biology. (abstract)
Wolf J, Reimer T, Schuck S, Rüder C, Gerlach K, Müller EC, Otto A, Dörken B, Rehm A (2010) Role of EBAG9 protein in coat protein complex I-dependent glycoprotein maturation and secretion processes in tumor cells. FASEB Journal. (abstract)
Schuck S, Prinz WA, Thorn KS, Voss C, Walter P (2009) Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. Journal of Cell Biology. (abstract)
Lingwood D, Schuck S, Ferguson C, Gerl MJ, Simons K (2009). Generation of cubic membranes by controlled homotypic interaction of membrane proteins in the endoplasmic reticulum. Journal of Biological Chemistry. (abstract)
Torkko JM, Manninen A, Schuck S, Simons K (2008). Depletion of apical transport proteins perturbs epithelial cyst formation and ciliogenesis. Journal of Cell Science. (abstract)
Schuck S*, Gerl MJ*, Ang AL, Manninen A, Keller P, Mellman I, Simons K (2007) Rab10 is involved in basolateral transport in polarized MDCK cells. Traffic. (abstract)
Schuck S*, Manninen A*, Honsho M, Füllekrug J, Simons K (2004) Generation of single and double knockdowns in polarized epithelial cells by retrovirus-mediated RNA interference. Proceedings of the National Academy of Sciences USA. (abstract)
Schuck S*, Honsho M*, Ekroos K, Shevchenko A, Simons K (2003) Resistance of cell membranes to different detergents. Proceedings of the National Academy of Sciences USA. (abstract)
Schuck S, Soloaga A, Schratt G, Arthur JS, Nordheim A (2003) The kinase MSK1 is required for induction of c-fos by lysophosphatidic acid in mouse embryonic stem cells. BMC Molecular Biology (abstract)
Schratt G, Weinhold B, Lundberg A, Schuck S, Berger J, Schwarz H, Weinberg R, Ruther U, Nordheim A (2001) Serum response factor is required for immediate-early gene activation yet is dispensable for proliferation of embryonic stem cells. Molecular and Cellular Biology. (abstract)
Reviews, commentaries and book chapters
Schuck S (2020) Microautophagy - distinct molecular mechanisms handle cargoes of many sizes. Journal of Cell Science. Review (abstract)
Schäfer JA, Schuck S (2020) ESCRTing endoplasmic reticulum to microautophagic degradation. Autophagy. Commentary (abstract)
Schäfer JA, Schuck S (2017) Biogenese und Autophagie des Endoplasmatischen Retikulums. BIOspektrum. Review, in German (abstract)
Schuck S (2016) On keeping the right ER size. Nature Cell Biology. Commentary (abstract)
Klionsky DJ, Abdelmohsen K, ..., Schuck S, ... Zughaier SM (2016). Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy. Review (abstract)
Lingwood D, Schuck S, Ferguson C, Gerl MJ, Simons K (2009) Morphological homeostasis by autophagy. Autophagy. Commentary (abstract)
Bernales S*, Schuck S*, Walter P (2007) ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy. Commentary (abstract)
Schuck S, Simons K (2006) Controversy fuels trafficking of GPI-anchored proteins. Journal of Cell Biology. Commentary (abstract)
Schuck S, Honsho M, Simons K (2006) Detergent-resistant membranes and the use of cholesterol depletion. In Cell Biology: A Laboratory Handbook, Volume 2. J. E. Celis, editor. Elsevier Science, USA. Book chapter (full text)
Schuck S, Simons K (2004) Polarized sorting in epithelial cells: raft clustering and the biogenesis of the apical membrane. Journal of Cell Science. Review (abstract)
Current Lab Members
| Sebastian Schuck 2013- |
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Sebastian still fantasizes about doing experiments himself, but the harsh reality is that he is stuck at the desk. sebastian.schuck@bzh.uni-heidelberg.de 06221-544749 |
| Saccharo Cerevis 2013- |
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Saccharo has been our resident oracle since the lab started in July 2013. What s/he says is mostly incomprehensible but sometimes reveals amazing insights. |
| Dimitris Papagiannidis 2016- |
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Dimitris started his master thesis with us in October 2016 and stayed for his PhD. He tries to understand the mechanisms that balance ER sheets and tubules, and also to find his balance while rock climbing. dimitrios.papagiannidis@bzh.uni-heidelberg.de 06221-545420 |
| Oliver Pajonk 2018- |
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Oli started his master thesis with us in September 2018 and stayed for his PhD to investigate ESCRTs. He enjoys playing music, running and convincing lab members to join running events together with him. oliver.pajonk@bzh.uni-heidelberg.de 06221-544688 |
| Giulia Ruffini 2018- |
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Giulia started her master thesis with us in November 2018 and stayed for her PhD to work on ER biogenesis. Besides science, Giulia has two great passions: music (she loves to sing) and food (cooking and eating). giulia.ruffini@bzh.uni-heidelberg.de 06221-544688 |
| Sibylle Kanngießer 2019- |
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Sibylle began her PhD in April 2019 to investigate SHRED. In her spare time, she relaxes doing yoga or joins other lab members for running or bouldering. sibylle.kanngiesser@bzh.uni-heidelberg.de 06221-544688 |
| Niklas Peters 2019- |
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Niklas started his PhD in April 2019 and wants to reconstitute SHRED in vitro. When not purifying proteins, he - you guessed it - goes running or bouldering. niklas.peters@bzh.uni-heidelberg.de 06221-544688 |
| Lis Albert 2020- |
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Lis started her Master thesis with us in January 2020 and stayed for her PhD to find out how ESCRT proteins talk with the ER. In her spare time, she enjoys many activities, including ... bouldering. lis.albert@bzh.uni-heidelberg.de 06221-544688 |
| Ayelén Valko 2020- |
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Ayelén joined us as a postdoc in October 2020 and is working on micro-ER-phagy. She is also a serious artist and composes science-inspired paintings, for example see this article. ayelen.valko@bzh.uni-heidelberg.de 06221-544688 |
| Anna Platzek 2021- |
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Anna started her PhD in April 2021 to find out what ER whorls are made of. She already knows exactly what coffee and cake should be made of. anna.platzek@bzh.uni-heidelberg.de 06221-545420 |
| Inge Reckmann 2021- |
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Inge never joined the lab - the lab joined her when we moved into the lab space that she had been looking after as a technician for many years. inge.reckmann@bzh.uni-heidelberg.de 06221-545420 |
| Anke Heymann 2021- |
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Anke is our administrative assistant. For our lab, she fights her way through the bureaucratic jungle, always building bridges between science and administration – and also between duty, coffee and cake. anke.heymann@bzh.uni-heidelberg.de 06221-544160 |
Former Lab Members
| Katharina Schaeff 2013-2017 |
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Katharina was our technician from September 2013 to October 2017. Besides maintaining the lab in good shape, Katharina worked on both SHRED and ER-phagy. |
| Tamas Szoradi 2013-2018 |
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Tamas did his PhD from October 2013 to March 2018, unravelling SHRED in all its glory. Tamas then moved to New York to do a postdoc with Liam Holt. |
| Jasmin Schäfer 2014-2020 |
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Jasmin did her PhD from August 2014 to Januar 2020. The force was strong with this one and Jasmin heroically cracked (some of) the secrets of micro-ER-phagy. She then moved to Frankfurt to do a postdoc with Christian Münch. |
| Dorottya Polos 2014-2015 |
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Dorottya was an ERASMUS student from October 2014 to June 2015. Afterwards, she returned to London to complete her Bachelor’s degree and do her PhD with Margaret Dallman. |
| Rolf Schmidt 2014-2019 |
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Rolf did his PhD from December 2014 to April 2019, investigating how cells adapt protein degradation capacity to stress. He then stayed in Heidelberg to do a postdoc with Carlos Bas Orth. |
| Peter Bircham 2015-2018 |
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Peter was a postdoc with us from February 2015 to September 2018 to study ER size control. Outside the lab, Peter still put yeast to good use brewing beer. This naturally led to his second postdoc with Kevin Verstrepen in Leuven, where Peter engineers better yeast for making beer. |
| Verena Bittl 2015 |
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Verena did her Master thesis from April to November 2015, exploring potential ER-phagy substrates. She moved to Frankfurt to pursue her PhD with Anja Bremm. |
| Julia Schessner 2017-2018 |
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Julia did her Master thesis from September 2017 to April 2018, visualizing and quantifying micro-ER-phagy by time lapse microscopy. For her PhD, Julia joined Georg Borner’s group at the MPI for Biochemistry in Munich. |
| Carlos Martìn de Hijas 2021 |
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Carlos did his Master thesis with us and looked at transcriptional responses to ER stress, mostly by staring at the computer screen. |
CV Sebastian Schuck
since 2021 Professor for Biochemistry and Molecular Cell Biology
Heidelberg University Biochemistry Center
2013-2021 Independent group leader
Center for Molecular Biology at Heidelberg University
2006-2013 Postdoctoral fellow with Peter Walter
University of California, San Francisco
2001-2006 PhD student and postdoctoral fellow with Kai Simons
Max Planck Institute of Molecular Cell Biology, Dresden
1995-2000 Biochemistry student
Universities of Hannover and Tübingen
Lab Pictures
August 2020. The lab in its natural environment.
From left to right: Oli, Niklas, Dimitris, Sebastian, Giulia, Sibylle, Lis and Uxia.
March 2020. Lab meeting in times of Corona.
February 2020. Jasmin has defended her PhD and even the dark side pays its respects.
September 2019, in deep thought at the lab retreat. From left to right: Jasmin, Giulia, Dimitris, Sebastian,
Niklas (apparently having an idea), Sibylle and Oli.
July 2019, the lab participates in the 10 K run of the National Center for Tumor Diseases. From left to
right: Oli, Niklas, Dimitris, Sebastian and Sibylle (we blame the red faces on the camera).
October 2018. From left to right: Oli, Sebastian, Giulia, Dimitris, Rolf, Jasmin and Carlos.
May 2018, the lab goes climbing. From left to right: Dimitris (giving instructions that Rolf can't see), Rolf,
Tamas and Peter.
September 2017. From left to right: Tamas, Katharina, Jasmin, Sebastian, Rolf, Peter, Julia and Dimitris.
June 2017, at the lab retreat. Dimitris, Peter and Jasmin draw up their (fantasy) papers.
May 2017. Is our ceiling going to withstand the construction work on the floor above us? Jasmin, Peter,
Tamas and Dimitris are not too sure.
June 2016, at the lab retreat. From left to right: Peter, Rolf, Tamas, Jasmin, Sebastian, Katharina, Julia and
Tanja.
February 2015. From left to right: Sebastian, Katharina, Peter, Rolf, Jasmin, Dorottya and Tamas.
Open Positions
We currently have no open positions, sorry.
Contact
Heidelberg University
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
Biochemistry Center (BZH)
Im Neuenheimer Feld 328
69120 Heidelberg
Office:
+49 6221 54-4749 Fax:
+49 6221 54-4366 E-Mail:
sebastian.schuck@bzh.uni-heidelberg.de 