simon.alberti@tu-dresden.de
© MPI-CBG
Expertise
The Alberti group studies how cells adapt to environmental stresses by assembling biomolecular condensates. The group applies biophysical, biochemical, genetic, and cell biological methods to investigate the molecular mechanisms of assembly and the functions of stress inducible condensates. Among others, the Alberti group has shown that condensate assembly regulates protein synthesis1-3, stress responses1,2,4,5,6 and the DNA damage response7,8. Most importantly, the Alberti group discovered together with the Hyman group that condensate-forming proteins can assemble into aberrant condensates that cause aging-associated diseases7,6,9,10. In collaboration with the Schlierf group, the Alberti group recently established a model for the assembly of RNP granules and their function in regulating RNA availability and translation.
References:
- Desroches Altamirano, Alberti et al. eIF4F is a thermo-sensing regulatory node in the translational heat shock response. Mol Cell. 2024;84(9):1727-1741.e12. https://doi.org/10.1016/j.molcel.2024.02.038
- Iserman, Alberti et al. Condensation of Ded1p Promotes a Translational Switch from Housekeeping to Stress Protein Production. Cell. 2020;181(4):818-831.e19. https://doi.org/10.1016/j.cell.2020.04.009
- Franzmann, Alberti et al. Phase separation of a yeast prion protein promotes cellular fitness. Science. 2018;359(6371):eaao5654. https://doi.org/10.1126/science.aao5654
- Guillén-Boixet, Alberti et al. RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation. Cell. 2020;181(2):346-361.e17. https://doi.org/10.1016/j.cell.2020.03.049
- Munder, Alberti et al. A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy. Singer RH, ed. eLife. 2016;5:e09347. https://doi.org/10.7554/eLife.09347
- Mateju , Alberti et al. An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. EMBO J. 2017;36(12):1669-1687. https://doi.org/10.15252/embj.201695957
- Patel, Alberti et al. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. Cell. 2015;162(5):1066-1077. https://doi.org/10.1016/j.cell.2015.07.047
- Chappidi, Alberti et al. PARP1-DNA co-condensation drives DNA repair site assembly to prevent disjunction of broken DNA ends. Cell. 2024;187(4):945-961.e18. https://doi.org/10.1016/j.cell.2024.01.015
- Wang, Alberti et al. A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins. Cell. 2018;174(3):688-699.e16. https://doi.org/10.1016/j.cell.2018.06.006
- Maharana S, Wang J, Papadopoulos DK, Richter D, Pozniakovsky A, Poser I, Bickle M, Rizk S, Guillén-Boixet J, Franzmann TM, Jahnel M, Marrone, Alberti et al. RNA buffers the phase separation behavior of prion-like RNA binding proteins. Science. 2018;360(6391):918-921. https://doi.org/10.1126/science.aar7366
Current news by this research group
Jahnel, Alberti, and Hyman among Clarivate’s Highly Cited Researchers in 2025
Left to right: Alberti, Jahnel, and Hyman
RTG 3120 PI's have been…