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• W2952431128 abstract "Volume-regulated anion channels (VRACs) are central to cell volume regulation. Recently identified as hetero-hexamers formed by LRRC8 proteins, their activation mechanism remains elusive. Here, we measured Förster resonance energy transfer (FRET) between fluorescent proteins fused to the C-termini of LRRC8 subunits. Inter-subunit FRET from LRRC8 complexes tracked VRAC activation. With patch-clamp fluorometry, we confirmed that the cytoplasmic domains rearrange during VRAC opening. With these FRET reporters, we determined VRAC activation, non-invasively, in live cells and their subcompartments. Reduced intracellular ionic strength did not directly activate VRACs, and VRACs were not activated on endomembranes. Instead, pharmacological manipulation of diacylglycerol (DAG), and protein kinase D (PKD) activity, activated or inhibited plasma membrane-localized VRACs. Finally, we resolved previous contradictory reports concerning VRAC activation, using FRET to detect robust activation by PMA that was absent during whole-cell patch clamp. Overall, non-invasive VRAC measurement by FRET is an essential tool for unraveling its activation mechanism." @default.
• W2952431128 created "2019-06-27" @default.
• W2952431128 creator A5005960069 @default.
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• W2952431128 date "2019-06-18" @default.
• W2952431128 modified "2023-10-03" @default.
• W2952431128 title "A FRET sensor of C-terminal movement reveals VRAC activation by plasma membrane DAG signaling rather than ionic strength" @default.
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• W2952431128 doi "https://doi.org/10.7554/elife.45421" @default.
• W2952431128 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6597245" @default.
• W2952431128 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31210638" @default.
• W2952431128 hasPublicationYear "2019" @default.
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