Unknown

Dataset Information

0

Differential PI(4,5)P2 sensitivities of TRPC4, C5 homomeric and TRPC1/4, C1/5 heteromeric channels.


ABSTRACT: Transient receptor potential canonical (TRPC) 4 and TRPC5 channels are modulated by the G?q-PLC pathway. Since phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) maintains TRPC4 and TRPC5 channel function, the G?q-PLC pathway inhibits channel activity by depleting PI(4,5)P2. Here we investigated the difference in PI(4,5)P2 sensitivity between homomeric and heteromeric TRPC channels. First, by using a Danio rerio voltage-sensing phosphatase (DrVSP), we show that PI(4,5)P2 dephosphorylation robustly inhibits TRPC4?, TRPC4?, and TRPC5 homotetramer currents and also TRPC1/4?, TRPC1/4?, and TRPC1/5 heterotetramer currents. Secondly, sensitivity of channels to PI(4,5)P2 dephosphorylation was suggested through the usage of FRET in combination with patch clamping. The sensitivity increased in the sequence TRPC4??

SUBMITTER: Ko J 

PROVIDER: S-EPMC6372716 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Differential PI(4,5)P<sub>2</sub> sensitivities of TRPC4, C5 homomeric and TRPC1/4, C1/5 heteromeric channels.

Ko Juyeon J   Myeong Jongyun J   Shin Young-Cheul YC   So Insuk I  

Scientific reports 20190212 1


Transient receptor potential canonical (TRPC) 4 and TRPC5 channels are modulated by the Gα<sub>q</sub>-PLC pathway. Since phosphatidylinositol 4,5-bisphosphate (PI(4,5)P<sub>2</sub>) maintains TRPC4 and TRPC5 channel function, the Gα<sub>q</sub>-PLC pathway inhibits channel activity by depleting PI(4,5)P<sub>2</sub>. Here we investigated the difference in PI(4,5)P<sub>2</sub> sensitivity between homomeric and heteromeric TRPC channels. First, by using a Danio rerio voltage-sensing phosphatase (D  ...[more]

Similar Datasets

| S-EPMC6381110 | biostudies-literature
| S-EPMC5599800 | biostudies-other
| S-EPMC4270102 | biostudies-literature
2022-03-26 | PXD031266 | Pride
| S-EPMC5717101 | biostudies-literature
| S-EPMC3409096 | biostudies-literature
| S-EPMC7501565 | biostudies-literature
| S-EPMC8262684 | biostudies-literature
| S-EPMC10699586 | biostudies-literature
| S-EPMC5665444 | biostudies-literature