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Simon Alberti – Cellular Biochemistry

We still know very little about the organization of the cytoplasm and the role of membraneless compartments in regulating the physiology of cells. My research group aims to elucidate the molecular principles underlying the organization of the cytoplasm. We are particularly interested in understanding how the cytoplasm changes upon environmental stress. Stressed cells have to adapt their physiology and metabolism to the new conditions. These adaptations are often mediated by alterations in the structure and organization of the cytoplasm. We aim to understand how these alterations promote organismal survival but we are also very interested in how they cause disease.

Curriculum Vitae


  • 2004 PhD in Biology, University of Bonn, Germany
  • 2000 Diploma in Biology, University of Bochum, Germany

Academic Career

  • Since 2018 Professor of Cellular Biochemistry at CMCB/BIOTEC
  • 2016 - 2018 Honorary Professor at Biotechnology Center (BIOTEC), Dresden
  • 2015 - 2016 Young Investigator at Technical University Dresden
  • 2010 - 2018 Group Leader at MPI of Molecular Cell Biology and Genetics, Dresden
  • 2005 - 2010 Postdoctoral work at Whitehead Institute, Cambridge, USA

Awards and Grants

  • 2017 ERC Consolidator Grant
  • 2017 Volkswagen Life? Grant
  • 2017 HFSP Program Grant
  • 2016 Coordinator JPND Grant CureALS
  • 2016 ASCB Gibco Emerging Leader Award
  • 2014 DIPP Outstanding PI Award
  • 2009 Margaret and Herman Sokol Postdoctoral Award
  • 2006 Research Fellowship of the DFG


The cytoplasm is a mysterious jelly-like substance that sustains the biochemical reactions that are essential for life. How the cytoplasm organizes itself is one of the big remaining questions in biology. We use cell biological, biochemical, biophysical and genetic approaches and diverse model systems, such as yeast, Dictyostelium, and mammalian cells, to elucidate the molecular principles underlying the organization of the cytoplasm. We are particularly interested in understanding how the cytoplasm reorganizes itself upon environmental perturbations and stress. Stressed cells undergo changes on many levels to alter their physiology and metabolism; we are beginning to understand that many of these changes result from alterations in the structure and organization of the cytoplasm.

Research focus of the Alberti lab. The figure shows an idealized cell that transitions into a different physiological state upon stress. This transition is associated with changes in the organization of the cytoplasm and the formation of liquid- or solid-like condensates (gels, glasses, or crystals). In unstressed cells, the molecules are not interacting with each other and can thus be considered to be in a gas-like state (Unassembled). However, upon stress, they assemble into a condensed state (Assembled). Thus, the overall process has hallmarks of a phase transition.

Our recent work shows that stressed cells form many membraneless compartments in the cytoplasm via a biophysical process known as phase separation. However, the initially beneficial ability to form compartments becomes detrimental with increasing age, because compartment-forming have a tendency to misfold and aggregate and thus are closely tied to aging and the pathogenesis associated with age-related diseases such as amyotrophic lateral sclerosis (ALS). Thus, recent efforts in the lab are focused on understanding the molecular links between membraneless compartments and age-related diseases.


Project 1: The chemistry and physics of the cytoplasm under stress

How do cells adapt to stress? We showed that the cytoplasm of stressed cells undergoes a phase transition from a liquid to a solid-like state (Munder et al., 2016). This phase transition is triggered by changes in physicochemical conditions such as fluctuations in cytosolic pH or temperature, which promote assembly of specific proteins and RNAs into cytoplasmic condensates.

What is the function of these condensates? We recently demonstrated that the yeast polyU-binding protein (Pub1) forms stress-protective condensates upon starvation or heat stress and that this is associated with cell cycle arrest (Kroschwald et al., 2018). Release from arrest coincides with condensate dissolution, which takes minutes (starvation) or hours (heat shock). The different dissolution rates of starvation- and heat-induced condensates are due to their different material properties: starvation-induced Pub1 condensates are reversible gels, whereas heat-induced condensates are solid-like and require chaperones for disassembly. Thus, different physiological stresses induce condensates with distinct physical properties and thereby define different modes of stress adaptation and rates of recovery.

In another recent study, we uncovered an unexpected function of the N-terminal prion domain of the canonical yeast prion protein and translation termination factor Sup35 (Franzmann et al., 2018). In stressed yeast, the Sup35 prion domain forms protective gels via pH-regulated phase separation followed by gelation (Figure 1). Gelation promotes cell survival by rescuing the essential translation factor from stress-induced damage. We propose that prion-like domains are protein-specific modifiers with chaperone-like functions that regulate protein phase behavior and protect proteins from damage.

Figure 1. Phase separation and gelation protects the essential translation termination factor Sup35 from stress-induced damage. (A) Sup35-GFP purified from insect cells forms liquid condensates in a pH-dependent manner. (B) Gel-like condensates of Sup35 as seen by Cryo-EM tomography. (C) Schematic describing the role of the N-terminal gel-forming domain (NM) of Sup35 during stress adaptation. In the presence of the gel-forming domain (left), Sup35 forms reversible gel condensates that protect the translation termination factor from damage. In the absence of the gel-forming domain (right), Sup35 forms irreversible aggregates that cause cell cycle arrest.

In the future, we aim to further characterize adaptive liquid-to-solid phase transitions of the cytoplasm. To this end, we will take a multi-scale approach, investigating these phase transitions on the level of entire cells, the cytoplasm and the level of macromolecules. We further aim to determine the function of various condensates that form when the cytoplasm solidifies. We hypothesize that condensate formation regulates the activity of proteins and protects proteins from damage, thus allowing stressed cells to adapt to the new environmental conditions, survive and recover from stress. We predict that this stress-protective system has similar significance as the well-established stress-protective system of molecular chaperones. More generally, we envisage that phase transitions are used across the kingdom of life to promote adaption to unfavorable environments. Future studies will therefore focus on the evolutionary forces that shape adaptive phase transitions in diverse organisms.

M. C. Munder, D. Midtvedt, T. Franzmann, E. Nüske, O. Otto, M. Herbig, E. Ulbricht, P. Müller, A. Taubenberger, S. Maharana, L. Malinovska, D. Richter, J. Guck, V. Zaburdaev, S. Alberti (2016). A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy. eLife, e09347, (2016).

S. Kroschwald, M. C. Munder, S. Maharana, T. M. Franzmann, D. Richter, M. Ruer, A. A. Hyman, S. Alberti. Different material states of Pub1 condensates define distinct modes of stress adaptation and recovery. Cell Reports, 23, 3327-3339, (2018).

T. M. Franzmann, M. Jahnel, A. Pozniakovsky, J. Mahamid, A. S. Holehouse, E. Nüske, D. Richter, W. Baumeister, S. W. Grill, R. V. Pappu, A. A. Hyman, S. Alberti. Phase separation of a yeast prion protein promotes cellular fitness. Science, 359, eaao5654, (2018).

Project 2: Membraneless compartments and disease-associated phase transitions

Proteins containing intrinsically disordered domains of low sequence complexity (also known as prion-like proteins) are frequently found in ribonucleoprotein (RNP) granules. What are the molecular properties of these proteins and what is their function? We demonstrated that the ALS-associated prion-like protein FUS forms dynamic RNP granules by liquid-liquid phase separation (Patel et al., 2015). We further found that liquid condensates assembled from patient-derived FUS show biophysical abnormalities and transition into an aberrant solid-like state. These findings suggest a molecular explanation for why these proteins are frequently associated with age-related diseases.

In another recent study, we used extensive mutagenesis to identify a sequence-encoded molecular grammar underlying the driving forces for phase separation of FUS and related proteins (Wang et al., 2018). We found that phase separation of these proteins is driven primarily by interactions amongst tyrosine residues in prion-like domains and arginine residues in RNA binding domains. This work opens the door to predicting phase separation properties based on primary amino acid sequence.

How is the phase behavior of FUS and related prion-like proteins regulated in cells? FUS is largely soluble in the nucleus but it forms solid pathological aggregates when mislocalized to the cytoplasm. We found that this is due to the regulation of the solubility of FUS by RNA (Maharana et al., 2018). Low RNA/protein ratios promote phase separation into liquid droplets, whereas high ratios prevent droplet formation in vitro (Figure 2). Reduction of nuclear RNA levels causes excessive phase separation and the formation of cytotoxic solid-like assemblies in cells. We propose that the nucleus is a buffered system in which high RNA concentrations keep FUS soluble. Furthermore, changes in RNA levels or RNA-binding abilities of FUS cause disease-causing aberrant phase transitions.

Figure 2.: RNA regulates the phase behaviour of the prion-like RNA-binding proteins FUS.FUS is in a diffuse and well-mixed state in the presence of high RNA concentrations but forms liquid condensates at intermediate RNA/protein ratios. Low RNA concentrations promote the conversion of FUS into a solid-like aggregated state.

In the future, we will investigate the phase behaviour of various disease-associated proteins. One important goal will be to dissect the molecular grammar of these proteins. This will allow us to determine how changes in the saturation concentration or material properties affect the biological function of condensates. In this context, we aim to understand on a deeper level how RNA regulates the phase behaviour of phase-separating proteins, focussing on features such as RNA multivalence and RNA secondary structure. Finally, we will investigate the role of ATP-driven machines such as molecular chaperones and helicases in regulating the material properties of condensates. By doing so, we hope to gain important insight into pathways that could delay the onset of age-related diseases.

A. Patel, H. K. Lee, L. Jawerth, S. Maharana, M. Jahnel, M. Y. Hein, S. Stoynov, J. Mahamid, S. Saha, T. Franzmann, A. Pozniakovski, I. Poser, N. Maghelli, L. Royer, M. Weigert, E. W. Myers, S. W. Grill, D. N. Drechsel, A. Hyman, S. Alberti. A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation. Cell, 162, 1066-1077, (2015).

J. Wang, J. Choi, A. S. Holehouse, X. Zhang, M. Jahnel, S. Maharana, R. Lemaitre, A. Pozniakovski, D. Drechsel, I. Poser, R. V. Pappu, S. Alberti, A. A. Hyman. A molecular grammar underlying the driving forces for phase separation of prion-like RNA binding proteins. Cell, 174, 688-699 (2018).

S. Maharana, J. Wang, D.K. Papadopoulos, D. Richter, A. Pozniakovsky, I. Poser, M. Bickle, S. Rizk, M. Jahnel, Y. T. Chang, P. Tomancak, A. A. Hyman, S. Alberti. RNA buffers the phase separation behavior of prion-like RNA-binding proteins. Science, eaar7366, (2018).


A complete list of publications can be found on Google scholar


  1. Jie Wang, Jeong-Mo Choi, Alex S Holehouse, Hyun O. Lee, Xiaojie Zhang, Marcus Jahnel, Shovamayee Maharana, Regis P. Lemaitre, Andrei I. Pozniakovsky, David N. Drechsel, Ina Poser, Rohit V Pappu, Simon Alberti, Anthony Hyman. A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins (2018). Cell, 174, doi: 10.1016/j.cell.2018.06.006.
  2. Simon Alberti, Shambaditya Saha, Jeffrey Woodruff, Titus Franzmann, Jie Wang, Anthony Hyman. A User's Guide for Phase Separation Assays with Purified Proteins (2018). J Mol Biol, doi: 10.1016/j.jmb.2018.06.038.
  3. Titus Franzmann, Simon Alberti. Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior (2018). J Biol Chem, doi: 10.1074/ jbc.TM118.001190
  4. Sonja Kroschwald, Matthias Munder, Shovamayee Maharana, Titus Franzmann, Doris Richter, Martine Ruer, Anthony Hyman, Simon Alberti. Different Material States of Pub1 Condensates Define Distinct Modes of Stress Adaptation and Recovery (2018). Cell Reports, 23(11) 3327-3339.
  5. S. Boeynaems, S. Alberti, N. L. Fawzi, T. Mittag, R. Parker, M. Polymenidou, F. Rousseau, J. Schymkowitz, J. Shorter, B. Wolozin, L. Van Den Bosch, P. Tompa, M. Fuxreiter (2018). Protein phase separation: a new phase in cell biology. Trends in Biochemical Sciences, 28(6) 420-435 (2018).
  6. Simon Alberti, Serena Carra. Quality Control of Membraneless Organelles (2018). J Mol Biol, Art. No. doi: 10.1016/j.jmb.2018.05.013.
  7. Shovamayee Maharana, Jie Wang, Dimitrios Papadopoulos, Doris Richter, Andrei I. Pozniakovsky, Ina Poser, Marc Bickle, Sandra Rizk, Jordina Guillén-Boixet, Titus Franzmann, Marcus Jahnel, Lara Marrone, Young-Tae Chang, Jared Sterneckert, Pavel Tomancak, Anthony Hyman, Simon Alberti. RNA buffers the phase separation behavior of prion-like RNA binding proteins (2018). Science, 360(6391) 918-921.
  8. E. E. Boczek, S. Alberti (2018). One domain fits all: Using disordered regions to sequester misfolded proteins. Journal of Cell Biology, doi: 10.1083/jcb.201803015.
  9. S. Alberti (2018). Guilty by association: mapping out the molecular sociology of droplet compartments. Molecular Cell, 69:349-351.
  10. L. Marrone, I. Poser, I. Casci, J. Japtok, P. Reinhardt, A. Janosch, C. Andree, H. O. Lee, C. Moebius, E. Koerner, L. Reinhardt, M. E. Cicardi, K. Hackmann, B. Klink, A. Poletti, S. Alberti, M. Bickle, A. Hermann, U. Pandey, A. A. Hyman, and J. L. Sterneckert (2018). Isogenic FUS-eGFP iPSC Reporter Lines Enable Quantification of FUS Stress Granule Pathology that Is Rescued by Drugs Inducing Autophagy. Stem Cell Report, 10(2):375-389.
  11. M. Mittasch, P. Groß, M. Nestler, A. W. Fritsch, C. Iserman, M. Kar, M. Munder, A. Voigt, S. Alberti, S. W. Grill, M. Kreysing (2018). Non-invasive perturbations of intracellular flow reveal physical principles of cell organization. Nature Cell Biology, 20:344-351.
  12. T. M. Franzmann, M. Jahnel, A. Pozniakovsky, J. Mahamid, A. S. Holehouse, E. Nüske, D. Richter, W. Baumeister, S. W. Grill, R. V. Pappu, A. A. Hyman, S. Alberti (2018). Phase separation of a yeast prion protein promotes cellular fitness. Science, 359, eaao5654.
  13. S. Alberti (2017). Phase separation in biology. Current Biology, 27(20), R1097-R1102.
  14. A. Hernández-Vega, M. Braun, L. Scharrel, M. Jahnel, S. Wegmann, B. T. Hyman, S. Alberti, S. Diez, A. A. Hyman (2017). Local nucleation of microtubule bundles through tubulin concentration into a condensed tau phase. Cell Reports, 20(10) 2304-2312.
  15. K. Rizzolo, J. Huen, A. Kumar, S. Phanse, J. Vlasblom, Y. Kakihara, H. A. Zeineddine, Z. Minic, J. Snider, W. Wang, C. Pons, T. V. Seraphim, E. E. Boczek, S. Alberti, M. Costanzo, C. L. Myers, I. Stagljar, C. Boone, M. Babu, Walid A. Houry (2017). Novel features of the chaperone cellular network revealed through systematic interaction mapping. Cell Reports, 20(11) 2735-2748.
  16. F. F. Morelli, D. S. Verbeek, J. Bertacchini, J. Vinet, L. Mediani, S. Marmiroli, G. Cenacchi, M. Nasi, S. De Biasi, J. F. Brunsting, J. Lammerding, E. Pegoraro, C. Angelini, R. Tupler, S. Alberti, S. Carra (2017). Aberrant compartment formation by HSPB2 mislocalizes lamin A and compromises nuclear integrity and function. Cell Reports, 20(9) 2100-2115.
  17. S. Alberti (2017). The wisdom of crowds: regulating cell function through condensed states of living matter. J Cell Science, jcs.200295, doi:10.1242/jcs.200295.
  18. Sonja Kroschwald, Simon Alberti (2017). Gel or Die: Phase Separation as a Survival Strategy. Cell, 168, 947-948.
  19. Serena Carra, Simon Alberti, et al. The growing world of small heat shock proteins: from structure to functions. Cell Stress Chaperones, 22, 601-611 (2017).
  20. D. Mateju, T. Franzmann, A. Patel, A. Kopach, H. O. Lee, S. Carra, A. A. Hyman, S. Alberti (2017). An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. EMBO Journal, e201695957.
  21. A. Patel, L. Malinovska, S. Saha, S. Alberti, Y. Krishnan, A. A. Hyman (2017). ATP is a biological hydrotrope. Science, 356, 753-756.
  22. S. Kroschwald, S. Maharana, S. Alberti (2017). Hexanediol: a chemical probe to investigate the material properties of membrane-less compartments. Science Matters.
  23. S. Alberti, D. Mateju, L. Mediani and S. Carra (2017). Granulostasis: protein quality control of RNP granules. Frontiers Molecular Neuroscience, 10 Art. No. 84.
  24. C. Rabouille and S. Alberti (2017). Cell adaptation upon stress: the emerging role of membrane-less compartments. Current Opinions in Cell Biology, 47, 34-42.
  25. S. Alberti and A. A. Hyman (2016). Are aberrant phase transitions a driver of cellular aging? BioEssays, 38, 959-968.
  26. M. Ganassi, D. Mateju, I. Bigi, L. Mediani, I. Poser, H. O. Lee, S. J. Seguin, F. F. Morelli, J. Vinet, G. Leo, O. Pansarasa, C. Cereda, A. Poletti, S. Alberti, S. Carra (2016). A surveillance function of the HSPB8-BAG3-HSP70 chaperone complex ensures stress granule integrity and dynamism. Molecular Cell, 63, 796-810.
  27. E. Boke, M. Ruer, M. H. Wuehr, M. Coughlin, S. P. Gygi, S. Alberti, D. Drechsel, A. A. Hyman, T. J. Mitchison (2016). Amyloid-like Self-Assembly of a Cellular Compartment. Cell, 166: 637-650.
  28. M. C. Munder, D. Midtvedt, T. Franzmann, E. Nüske, O. Otto, M. Herbig, E. Ulbricht, P. Müller, A. Taubenberger, S. Maharana, L. Malinovska, D. Richter, J. Guck, V. Zaburdaev, S. Alberti (2016). A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy. eLife, 5:e09347.
  29. L. Malinovska and S. Alberti (2015). Protein misfolding in Dictyostelium: using a freak of nature to gain insight into a universal problem. Prion, DOI: 10.1080/ 19336896.2015.1099799.
  30. S. Alberti (2015). Don't Go with the Cytoplasmic Flow. Developmental Cell, 34:381-382.
  31. A. Patel, H. K. Lee, L. Jawerth, S. Maharana, M. Jahnel, M. Y. Hein, S. Stoynov, J. Mahamid, S. Saha, T. Franzmann, A. Pozniakovski, I. Poser, N. Maghelli, L. Royer, M. Weigert, E. W. Myers, S. W. Grill, D. N. Drechsel, A. Hyman, S. Alberti (2015). A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. Cell, 162(5), 1066-1077.
  32. S. Kroschwald, S. Maharana, D. Mateju, L. Malinovska, E. Nüske, I. Poser, D. Richter, S. Alberti (2015). Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules. eLife, 4, e06807.
  33. L. Malinovska, S. Palm, K. Gibson, J. Verbavatz, S. Alberti (2015). Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation. PNAS, April, 112(20), 2620-2629.
  34. M. Coelho, S. Lade, S. Alberti, T. Gross, I. M. Tolic-Nørrelykke (2014). Fusion of protein aggregates facilitates asymmetric damage segregation. PLoS Biology, DOI: 10.1371/journal.pbio.1001886.
  35. C. Rogon, A. Ulbricht, M. Hesse, S. Alberti, P. Vijayaraj, D. Best, I. R. Adams, T. M. Magin, B. K. Fleischmann, J. Höhfeld (2014). HSP70 Binding Protein HSPBP1 Regulates Chaperone Expression at a Posttranslational Level and is Essential for Spermatogenesis. Molecular Biology of the Cell, 25:2260-2271.
  36. I. Petrovska, E. Nüske, M. C. Munder, G. Kulasegaran, L. Malinovska, S. Kroschwald, D. Richter, K. Fahmy, K. Gibson, J. M. Verbavatz, Alberti S (2014). Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation. eLife, DOI: 10.7554/eLife.02409.001.
  37. M. Coelho, A. Dereli, A. Haese, S. Kuhn, L. Malinovska, M.E. DeSantis, J. Shorter, S. Alberti, T. Gross, I.M. Tolic-Nørrelykke (2013). Fission yeast does not age under favorable conditions but does so after stress. Current Biology, 23:1844-1852.
  38. S. Alberti (2013). Aggregating the message to control the cell cycle. Developmental Cell, 25:551-552.
  39. S. Tenreiro, M. Munder, S. Alberti, T.F. Outeiro (2013). Harnessing the power of yeast to unravel the molecular basis of neurodegeneration. Journal of Neurochemistry, DOI: 10.1111/jnc.12271.
  40. L. Malinovska, S. Kroschwald, S. Alberti (2013). Protein disorder, prion propensities, and self-organizing macromolecular collectives. BBA, 1834:918-931.
  41. P. Picotti, M. Clément-Ziza, H.Y.K. Lam, D.S. Campbell, A. Schmidt, E.W. Deutsch, H. Röst, Z. Sun, O. Rinner, L. Reiter, Q. Shen, J.J. Michaelson, A. Frei, S. Alberti, U. Kusebauch, B. Wollscheid, R.L. Moritz, A. Beyer, R. Aebersold (2013). A complete mass-spectrometric map of the yeast proteome applied to quantitative trait analysis. Nature, 494:266-270.
  42. S. Alberti (2012). Molecular mechanisms of spatial protein quality control. Prion, 6:437-442.
  43. R. Halfmann, J. Wright, S. Alberti, S. Lindquist, M. Rexach (2012). Prion formation by a yeast GLFG nucleoporin. Prion, 6:1-9.
  44. L. Malinovska, S. Kroschwald, M. C. Munder, D. Richter, S. Alberti (2012). Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Molecular Biology of the Cell, 23:3041-3056.
  45. R. Halfmann, S. Alberti, R. Krishnan, N. Lyle, C.W. O’Donnell, O.D. King, B. Berger, R. V. Pappu, S. Lindquist (2011). Opposing effects of glutamine and asparagine dictate prion formation by intrinsically disordered proteins. Molecular Cell, 43:72-84.
  46. S. Alberti, R. Halfmann, S. Lindquist (2010). Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast. Methods in Enzymology, 470:709-734.
  47. R. Halfmann, S. Alberti, S. Lindquist (2010). Prions, protein homeostasis, and phenotypic diversity. Trends in Cell Biology, 20:125-133.
  48. S. Alberti, R. Halfmann, O. King, A. Kapila, S. Lindquist (2009). A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell, 137:146-158.
  49. S. Alberti, A. Gilter, S. Lindquist (2007). A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast, 24:913-919.
  50. G. Grelle, S. Kostka, A. Otto, B. Kersten, K. F. Genser, E. C. Müller, S. Walter, A. Boddrich, U. Stelzl, C. Hanig, R. Volkmer-Engert, C. Landgraf, S. Alberti, J. Höhfeld, M. Strodicke, E. E. Wanker (2006). Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Molecular and Cellular Proteomics, 5:234-244.
  51. V. Arndt, C. Daniel, W. Nastinczyk, S. Alberti, J. Höhfeld (2005). BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP. Molecular Biology of the Cell, 16:5891-5900.
  52. S. Alberti, K. Böhse, V. Arndt, A. Schmitz, J. Höhfeld (2004). The co-chaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Molecular Biology of the Cell, 15:4003-4010.
  53. C. Esser, S. Alberti, J. Höhfeld (2004). Cooperation of molecular chaperones with the ubiquitin/proteasome system. Biochimica et Biophysica acta, 1695:171-88.
  54. S. Alberti, C. Esser, J. Höhfeld (2003). BAG-1 – a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones, 8:225-231.
  55. S. Alberti, J. Demand, C. Esser, N. Emmerich, H. Schild, J. Höhfeld (2002). Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. Journal of Biological Chemistry, 277: 45920-45927.
  56. S. Alberti, J. Höhfeld (2002). Molecular chaperones in the regulation of signal transduction. Ann N Y Acad Sci, 973:3-4.
  57. J. Demand, S. Alberti, C. Patterson, J. Höhfeld (2001). Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Current Biology, 11:1569-1577.


We gratefully acknowledge funding by the following organizations.

Group Members

You can find a list of current group members here.

Open Positions

We are always looking for highly motivated and creative students.

Students interested in a master’s project with a focus on biochemistry, biophysics or cell biology are encouraged to apply.

Students interested in a PhD project should apply to the Dresden International Graduate School for Biomedicine and Bioengineering (DIGS-BB) or they can apply directly to the lab as a Bioscience PhD student (BiPS).

We are also supporting fellowship applications of outstanding postdoctoral researchers who wish to join our lab. Funding is available through various organizations (Humboldt foundation, HFSP, EMBO, DAAD, etc.).

International students and researchers are particularly encouraged to get in touch.

In case you are interested in working with us please contact Simon Alberti.


Prof. Dr. Simon Alberti
Technische Universität Dresden
Biotechnology Center
Tatzberg 47/49
01307 Dresden, Germany
Email: Simon.Alberti(at)tu-dresden.de
Tel: +49 (0)351 463 40236
Fax: +49 (0)351 463 40244

Katharina Mähne
Administrative Assistant
Technische Universität Dresden
Biotechnology Center
Tatzberg 47/49
01307 Dresden, Germany
Tel: +49 (0)351 463 40236
Fax: +49 (0)351 463 40244

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