Membrane surfaces regulate assembly of ribonucleoprotein condensates.
Journal
Nature cell biology
ISSN: 1476-4679
Titre abrégé: Nat Cell Biol
Pays: England
ID NLM: 100890575
Informations de publication
Date de publication:
04 2022
04 2022
Historique:
received:
27
05
2021
accepted:
03
03
2022
revised:
26
01
2022
pubmed:
13
4
2022
medline:
27
4
2022
entrez:
12
4
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35411085
doi: 10.1038/s41556-022-00882-3
pii: 10.1038/s41556-022-00882-3
pmc: PMC9035128
mid: NIHMS1786109
doi:
Substances chimiques
Ribonucleoproteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
461-470Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM081506
Pays : United States
Organisme : NIGMS NIH HHS
ID : F32 GM136055
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Nature Limited.
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