Simon Alberti

Summary

Affiliation: Max Planck Institute of Molecular Cell Biology and Genetics
Country: Germany

Publications

  1. pmc Are aberrant phase transitions a driver of cellular aging?
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    Bioessays 38:959-68. 2016
  2. doi An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.
    Daniel Matějů
    EMBO J . 2017
  3. doi Don't Go with the Cytoplasmic Flow
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany Electronic address
    Dev Cell 34:381-2. 2015
  4. doi Aggregating the message to control the cell cycle
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
    Dev Cell 25:551-2. 2013
  5. pmc Molecular mechanisms of spatial protein quality control
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    Prion 6:437-42. 2012
  6. pmc Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
    Sonja Kroschwald
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    elife 4:e06807. 2015
  7. doi A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
    Avinash Patel
    Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany
    Cell 162:1066-77. 2015
  8. pmc A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy
    Matthias Christoph Munder
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    elife 5:. 2016
  9. pmc Fusion of protein aggregates facilitates asymmetric damage segregation
    Miguel Coelho
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany FAS Center for Systems Biology, Harvard University, Cambridge, Massachusetts, United States of America
    PLoS Biol 12:e1001886. 2014
  10. doi Protein disorder, prion propensities, and self-organizing macromolecular collectives
    Liliana Malinovska
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    Biochim Biophys Acta 1834:918-31. 2013

Collaborators

  • Titus M Franzmann
  • Serena Carra
  • Nicola Maghelli
  • Iva M Tolić-Nørrelykke
  • James Shorter
  • Liliana Malinovska
  • Shovamayee Maharana
  • Sonja Kroschwald
  • Miguel Coelho
  • Daniel Matějů
  • Avinash Patel
  • Doris Richter
  • Anthony A Hyman
  • Hyun O Lee
  • Matthias Christoph Munder
  • Elisabeth Nüske
  • Ina Poser
  • Thilo Gross
  • Edgar E Boczek
  • Andrii Kopach
  • Vasily Zaburdaev
  • Daniel Midtvedt
  • Jochen Guck
  • Oliver Otto
  • Anna Taubenberger
  • Maik Herbig
  • Elke Ulbricht
  • PAUL MULLER
  • Stoyno Stoynov
  • Sandra Palm
  • Stephan Grill
  • Andrej Pozniakovski
  • Jean Marc Verbavatz
  • Julia Mahamid
  • Kimberley Gibson
  • Marco Y Hein
  • David Drechsel
  • Eugene W Myers
  • Shambaditya Saha
  • Marcus Jahnel
  • Loic A Royer
  • Louise Jawerth
  • Martin Weigert
  • Iva M Tolić
  • Steven J Lade
  • Morgan E Desantis
  • Aygül Dereli
  • Sebastian Kuhn
  • Anett Haese
  • Matthias C Munder

Detail Information

Publications13

  1. pmc Are aberrant phase transitions a driver of cellular aging?
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    Bioessays 38:959-68. 2016
    ..We generalize this idea to suggest that the process of cellular aging involves a progressive loss of the organization of phase-separated compartments in the cytoplasm. ..
  2. doi An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.
    Daniel Matějů
    EMBO J . 2017
    ..Thus, cells employ a system of SG quality control to prevent accumulation of misfolded proteins and maintain the dynamic state of SGs, which may have relevance for ALS and related diseases...
  3. doi Don't Go with the Cytoplasmic Flow
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany Electronic address
    Dev Cell 34:381-2. 2015
    ..2015) report that streaming creates subcellular compartments in the filamentous fungus Neurospora crassa. Nuclei immobilized within these compartments differentiate and may drive a compartment-specific genetic program...
  4. doi Aggregating the message to control the cell cycle
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
    Dev Cell 25:551-2. 2013
    ..2013) report that the RNA-binding protein Whi3 spatially constrains a cyclin-encoding mRNA in the cytoplasm of multinucleate cells, thus allowing independent cell-cycle control of individual nuclei. ..
  5. pmc Molecular mechanisms of spatial protein quality control
    Simon Alberti
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    Prion 6:437-42. 2012
    ..These findings demonstrate that yeast cells can control the amount of soluble misfolded proteins through regulated phase transitions in the cytoplasm, thus allowing them to rapidly adapt to changing environmental conditions...
  6. pmc Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
    Sonja Kroschwald
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    elife 4:e06807. 2015
    ..Thus, we propose that the material state of RNP granules is flexible and that the solid state of yeast stress granules is an adaptation to extreme environments, made possible by the presence of a powerful disaggregation machine. ..
  7. doi A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
    Avinash Patel
    Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany
    Cell 162:1066-77. 2015
    ....
  8. pmc A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy
    Matthias Christoph Munder
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    elife 5:. 2016
    ....
  9. pmc Fusion of protein aggregates facilitates asymmetric damage segregation
    Miguel Coelho
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany FAS Center for Systems Biology, Harvard University, Cambridge, Massachusetts, United States of America
    PLoS Biol 12:e1001886. 2014
    ..Our work shows that fusion of protein aggregates promotes the formation of damage-free cells. Fusion of cellular factors may represent a general mechanism for their asymmetric segregation at division...
  10. doi Protein disorder, prion propensities, and self-organizing macromolecular collectives
    Liliana Malinovska
    Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
    Biochim Biophys Acta 1834:918-31. 2013
    ..This article is part of a Special Issue entitled: The emerging dynamic view of proteins: Protein plasticity in allostery, evolution and self-assembly...
  11. pmc Fission yeast does not age under favorable conditions, but does so after stress
    Miguel Coelho
    Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
    Curr Biol 23:1844-52. 2013
    ..In budding yeast, asymmetric segregation of cellular damage results in aging mother cells and rejuvenated daughters. We hypothesize that the organisms in which this asymmetry is lacking, or can be modulated, may not undergo aging...
  12. pmc Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation
    Liliana Malinovska
    Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany
    Proc Natl Acad Sci U S A 112:E2620-9. 2015
    ..Our data suggest that D. discoideum has undergone specific adaptations that increase the proteostatic capacity of this organism and allow for an efficient regulation of its prion-like proteome. ..
  13. pmc Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
    Liliana Malinovska
    Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany
    Mol Biol Cell 23:3041-56. 2012
    ..Our model suggests that protein aggregation is not a haphazard process but rather an orchestrated cellular response that adjusts the flux of misfolded proteins to the capacities of the protein quality control system...