Arabidopsis AUTOPHAGY-RELATED3 (ATG3) facilitates the liquid-liquid phase separation of ATG8e to pro

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In each cell,various components/organelles (including mem-branous and non-membranous organelles) assemble at the proper time and space to function.How organelles lacking a membrane form and the physicochemical natures of such organelles remain unknown.Recent studies have shown that membrane-free struc-tures can assemble by liquid-liquid phase separation (LLPS),an essential process in which protein molecules condense into a closed liquid compartment with other proteins or RNAs after they reach a critical threshold concentration [1].These components show highly sensitive fluidity and dynamic exchange with their surrounding liquid environments.LLPS plays crucial roles in vari-ous physiological and signaling processes by creating a relatively independent spatial domain to selectively enrich molecules and form distinct structures.Phase separation of SORTING OF cpTat SUBSTRATES TO THYLAKOID MEMBRANES1 (STT1) and STT2,key protein transport sorting factors to the chloroplast stroma,drives protein sorting in chloroplasts [2].Arabidopsis thaliana EARLY FLOWERING3 (ELF3) senses changes in ambient temperature through prion-like domain (PrD)-mediated phase transition [3].Two members of the plant guanylate-binding protein-like GTPase(GBPL) superfamily,GBPL1 and GBPL3,mobilize the host immune response to pathogen infection through phase transition,thereby enabling host defense [4].The prion-like protein FLOE1 (a name inspired by ice floes,which are sheets of floating ice and,thus,phase-separated bodies of water) regulates seed germination by sensing changes in environmental moisture through phase separa-tion [5].
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