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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| Vydáno v: | Science (American Association for the Advancement of Science) Ročník 373; číslo 6560; s. 1218 |
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| Hlavní autoři: | , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
United States
10.09.2021
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| Témata: | |
| ISSN: | 1095-9203, 1095-9203 |
| On-line přístup: | Zjistit podrobnosti o přístupu |
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| Shrnutí: | 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. |
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| Bibliografie: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ISSN: | 1095-9203 1095-9203 |
| DOI: | 10.1126/science.abg7071 |