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• W3019046983 abstract "Transient receptor potential canonical (TRPC)4 and TRPC5 channels are non-selective calciumpermeable cation channels that maintained by phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and inactivated due to its depletion. Phospholipase C (PLC) is an enzyme that cleaves phospholipids and the PLCδ is the most calcium-sensitive form among the isozymes that stimulated by physiological concentration of Ca2+. Here, we investigated the regulation mechanism of TRPC4 by the Ca2+-PLCδ-PI(4,5)P2 signaling cascade. In order to identify the interaction between ion channel and PLCδ protein, we implied co-immunoprecipitation and fluorescence imaging including Föster Resonance Energy Transfer. We evaluated the activity of channels with electrophysiological recording in HEK293 cells expressing TRPC channels. Here, we demonstrate that TRPC4 directly interacts with PLCδ1. We also found that PLCδ isozymes are activated by the calcium through opened channels but not by the cytosolic calcium increase. Our study established the PLCδ1 inhibits overall TRPC4’s currents activity, but mainly regulates the basal TRPC4 currents to have a characteristic low basal activity. These regulation of PLCδ1 on TRPC4 activity occurs depend on PI(4,5)P2 hydrolysis. Resultantly, PLCδ1 is considered to be a negative regulator of TRPC4. Support or Funding Information This research was supported by the National Research Foundation of Korea, which is funded by the Ministry of Science, ICT (Information & Communication Technology), and Future Planning (MSIP) of the Korean government (2018R1A4A1023822 to I.S.S.). H.Kang, J.Ko., J.Myeong., and M.Kwak. were supported by the BK plus program from the MSIP." @default.
• W3019046983 created "2020-05-01" @default.
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• W3019046983 date "2020-04-01" @default.
• W3019046983 modified "2023-09-24" @default.
• W3019046983 title "Regulation of transient receptor potential canonical 4 activity by phospholipase C δ1" @default.
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• W3019046983 doi "https://doi.org/10.1096/fasebj.2020.34.s1.09564" @default.
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