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• W4361212246 endingPage "6289" @default.
• W4361212246 startingPage "6289" @default.
• W4361212246 abstract "Physiological activation by light of the Drosophila TRP and TRP-like (TRPL) channels requires the activation of phospholipase Cβ (PLC). The hydrolysis of phosphatidylinositol 4,5, bisphosphate (PIP2) by PLC is a crucial step in the still-unclear light activation, while the generation of Diacylglycerol (DAG) by PLC seems to be involved. In this study, we re-examined the ability of a DAG analogue 1-oleoyl-2-acetyl-sn-glycerol (OAG) to activate the TRPL channels expressed in HEK cells. Unlike previous studies, we added OAG into the cytosol via a patch-clamp pipette and observed robust activation of the expressed TRPL channels. However, TRPL channel activation was much slower than the physiologically activated TRPL by light. Therefore, we used a picosecond-fast optically activated DAG analogue, OptoDArG. Inactive OptoDArG was added into the intracellular solution with the patch-clamp pipette, and it slowly accumulated on the surface membrane of the recorded HEK cell in the dark. A fast application of intense UV light to the recorded cell resulted in a robust and relatively fast TRPL-dependent current that was greatly accelerated by the constitutively active TRPLF557I pore-region mutation. However, this current of the mutant channel was still considerably slower than the native light-induced TRPL current, suggesting that DAG alone is not sufficient for TRPL channel activation under physiological conditions." @default.
• W4361212246 created "2023-03-31" @default.
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• W4361212246 date "2023-03-27" @default.
• W4361212246 modified "2023-10-14" @default.
• W4361212246 title "Diacylglycerol Activates the Drosophila Light Sensitive Channel TRPL Expressed in HEK Cells" @default.
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• W4361212246 doi "https://doi.org/10.3390/ijms24076289" @default.
• W4361212246 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37047261" @default.
• W4361212246 hasPublicationYear "2023" @default.
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