Regulation of biomolecular condensates by interfacial protein clusters

Biomolecular condensates are cellular compartments that can form by phase separation in the absence of limiting membranes. Studying the P granules of , we find that condensate dynamics are regulated by protein clusters that adsorb to the condensate interface. Using in vitro reconstitution, live obse...

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Veröffentlicht in:Science (American Association for the Advancement of Science) Jg. 373; H. 6560; S. 1218
Hauptverfasser: Folkmann, Andrew W, Putnam, Andrea, Lee, Chiu Fan, Seydoux, Geraldine
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States 10.09.2021
Schlagworte:
Animals
Caenorhabditis elegans - metabolism
Caenorhabditis elegans - physiology
Caenorhabditis elegans Proteins - metabolism
Intrinsically Disordered Proteins - metabolism
Oocytes - metabolism
Protein-Tyrosine Kinases - metabolism
RNA-Binding Proteins - metabolism
Zygote - metabolism
ISSN:1095-9203, 1095-9203
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Zusammenfassung:Biomolecular condensates are cellular compartments that can form by phase separation in the absence of limiting membranes. Studying the P granules of , we find that condensate dynamics are regulated by protein clusters that adsorb to the condensate interface. Using in vitro reconstitution, live observations, and theory, we demonstrate that localized assembly of P granules is controlled by MEG-3, an intrinsically disordered protein that forms low dynamic assemblies on P granules. Following classic Pickering emulsion theory, MEG-3 clusters lower surface tension and slow down coarsening. During zygote polarization, MEG-3 recruits the DYRK family kinase MBK-2 to accelerate spatially regulated growth of the P granule emulsion. By tuning condensate-cytoplasm exchange, interfacial clusters regulate the structural integrity of biomolecular condensates, reminiscent of the role of lipid bilayers in membrane-bound organelles.
Bibliographie:ObjectType-Article-1
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ISSN:1095-9203
1095-9203
DOI:10.1126/science.abg7071