Authors:

Victoria Isabella Porter

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About Paper:

Phospholipase C (PLC) is a family of enzymes that hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) at the plasma membrane. When a ligand binds to a G protein-coupled receptors (GPCR), G?q/11 disassociates from G?? then binds and activates PLCs causing the hydrolysis of PIP2 into diacylglycerol and inositol triphosphate (IP3). In mammalian PLCs, there is a subfamily called PLC? which includes PLC?1-4, all of which are activated by G?q/11 but only PLC?1-3 are activated by G??. It was unknown if PLC?4 interacted with G??, however, the constituently active D-to-Y mutation at position 630 is potentially inhibited by G??, showing that PLC?4 may interact with G??. To see if the effect of G?? is specific to PLC?4 or specific to the mutation, we are introducing the D-to-Y mutation to PLC?1-3 and performing an in cellulo assay to determine the activity with and without G?q/11 and G??. We expect to see an increase in basal activity in PLC?1-3 with the D-to-Y mutation compared to wild-type. However, we don't expect to see further increase nor decrease in activity when adding either G?q/11 or G??, thus rendering the mutated PLC?1-3 isoforms maximally active. This would show that the effect of G?? is specific to PLC?4 and not specific to the D-to-Y mutation. Keywords: Phospholipase C; Inositol Triphosphate; Heterotrimeric G Protein; GPCR; PIP2

Source:

Purdue University / 2025

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Co-authors:

Victoria Isabella Porter