The study examines the behavior of the focal adhesion protein p130Cas and its ability to undergo liquid-liquid phase separation (LLPS) in cells. Key findings:
p130Cas, which contains intrinsically disordered regions, forms dynamic cytoplasmic condensates that bud off from focal adhesions. These condensates exhibit typical LLPS characteristics like fusion, fission, and rapid exchange of components.
The p130Cas condensates contain other focal adhesion proteins like paxillin and FAK, as well as mRNAs and RNA-binding proteins involved in mRNA translation regulation.
Induction of large focal adhesions by plating cells on high concentrations of fibronectin leads to increased p130Cas condensate formation and suppression of global protein translation. This effect is dependent on p130Cas.
Optogenetic induction of p130Cas condensates using a light-sensitive Cry2 system also reduces translation, directly linking p130Cas LLPS to translational regulation.
Analysis of the mRNA content in the p130Cas condensates reveals enrichment of transcripts involved in cell cycle, survival, and cell-cell communication, many of which are also differentially regulated upon p130Cas overexpression.
These results identify a novel mechanism by which integrin-mediated adhesion can regulate mRNA translation through the formation of p130Cas-driven liquid-liquid phase separated condensates in the cytoplasm.
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by Kumar,A., Sc... في www.biorxiv.org 11-22-2023
https://www.biorxiv.org/content/10.1101/2023.11.22.568289v1استفسارات أعمق