Membrane surfaces regulate assembly of ribonucleoprotein condensates.

Autor: Snead WT; Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA., Jalihal AP; Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA., Gerbich TM; Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA., Seim I; Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.; Curriculum in Bioinformatics and Computational Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.; Department of Applied Physical Sciences, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA., Hu Z; Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA., Gladfelter AS; Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. amyglad@unc.edu.; Marine Biological Laboratory, Woods Hole, MA, USA. amyglad@unc.edu.
Jazyk: angličtina
Zdroj: Nature cell biology [Nat Cell Biol] 2022 Apr; Vol. 24 (4), pp. 461-470. Date of Electronic Publication: 2022 Apr 11.
DOI: 10.1038/s41556-022-00882-3
Abstrakt: Biomolecular condensates organize biochemistry, yet little is known about how cells control the position and scale of these structures. In cells, condensates often appear as relatively small assemblies that do not coarsen into a single droplet despite their propensity to fuse. Here, we report that ribonucleoprotein condensates of the glutamine-rich protein Whi3 interact with the endoplasmic reticulum, which prompted us to examine how membrane association controls condensate size. Reconstitution revealed that membrane recruitment promotes Whi3 condensation under physiological conditions. These assemblies rapidly arrest, resembling size distributions seen in cells. The temporal ordering of molecular interactions and the slow diffusion of membrane-bound complexes can limit condensate size. Our experiments reveal a trade-off between locally enhanced protein concentration at membranes, which favours condensation, and an accompanying reduction in diffusion, which restricts coarsening. Given that many condensates bind endomembranes, we predict that the biophysical properties of lipid bilayers are key for controlling condensate sizes throughout the cell.
(© 2022. The Author(s), under exclusive licence to Springer Nature Limited.)
Databáze: MEDLINE
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