The role of liquid–liquid phase separation in regulating enzyme activity |
| |
| Institution: | 1. Quantitative Biology and Bioinformatics, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany;2. Max Planck Institute for Dynamics and Self-Organization, Am Fassberg 17, 37077 Göttingen, Germany;3. Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany;1. Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;2. Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA;3. Research Institute of Molecular Pathology, Campus-Vienna-Biocenter 1, 1030 Vienna, Austria;1. Department of Genetics, Stanford University School of Medicine, Stanford, CA, USA;2. KU Leuven, Department of Neurosciences, Experimental Neurology and Leuven Research Institute for Neuroscience and Disease (LIND), Leuven, Belgium;3. VIB, Center for Brain and Disease Research, Laboratory of Neurobiology, Leuven, Belgium;4. Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany;5. Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, RI, USA;6. Department of Structural Biology, St. Jude Children’s Research Hospital, Memphis, TN, USA;7. Institute of Molecular Life Sciences, University of Zürich, Zürich, Switzerland;8. Switch Laboratory, VIB, Leuven, Belgium;9. KU Leuven, Department for Cellular and Molecular Medicine, Leuven, Belgium;10. Department of Biochemistry and Biophysics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA, USA;11. Department of Pharmacology, Boston University School of Medicine, Boston, MA, USA;12. Department of Neurology, Boston University School of Medicine, Boston, MA, USA;13. VIB, Center for Structural Biology (CSB), Vrije Universiteit Brussel (VUB), Brussels, Belgium;14. Institute of Enzymology, Research Centre for Natural Sciences of the Hungarian Academy of Sciences, Budapest, Hungary;15. MTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary;1. Program in Molecular Structure and Function, Hospital for Sick Children, Toronto, Ontario, Canada;2. Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada;1. Department of Cell and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;2. Cell and Tissue Imaging Center, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;3. Department of Structural Biology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;4. Howard Hughes Medical Institute, Department of Cell and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA;1. Department of Molecular & Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan;2. Department of Computational Medicine & Bioinformatics, University of Michigan Medical School, Ann Arbor, Michigan;3. Brehm Center for Diabetes Research, University of Michigan Medical School, Ann Arbor, Michigan |
| |
| Abstract: | Liquid–liquid phase separation (LLPS) is now recognized as a common mechanism underlying regulation of enzyme activity in cells. Insights from studies in cells are complemented by in vitro studies aimed at developing a better understanding of mechanisms underlying such control. These mechanisms are often based on the influence of LLPS on the physicochemical properties of the enzyme's environment. Biochemical mechanisms underlying such regulation include the potential for concentrating reactants together, tuning reaction rates, and controlling competing metabolic pathways. LLPS is thus a powerful tool with extensive utilities at the cell's disposal, e.g. for consolidating cell survival under stress or rerouting metabolic pathways in response to the energy state of the cell. Here, we examin the evidence for how LLPS affects enzyme catalysis and begin to understand emerging concepts and expand our understanding of enzyme catalysis in living cells. |
| |
| Keywords: | Membraneless organelles Biomolecular condensate Crowding Catalysis Metabolism Stress response |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
