Master phosphatase
Protein phosphatase 2A (PP2A)
Also searched as Protein phosphatase 2A (PP2A).
You want it held back, and it is the true off-switch. Deleting the messenger and quieting the kinase do not by themselves stop the process — cessation ultimately depends on removing the phosphate marks, and that is what this does. The elegant cruelty: the kinase that starts the process also switches this on, so the accelerator arms the brake. And ceramides activate it too, which is how a lipid species you may be carrying too much of quietly ends fat release.
In depth
The phosphatase that strips the activating marks off the lipase and the coat, ending release.
What drives it
Lipolysis signal increases it.
The accelerator arms the brake. 'Multiple studies have suggested that pp2a can be activated by the cAMP-PKA pathway via phosphorylation of the regulatory subunit. It seems likely that PKA-PP2A-dependent dephosphorylation may contribute to a negative feedback loop that counterbalances PKA-dependent phosphorylation'. doi 10.3389/fphys.2022.826314
Ceramide load increases it.
A cross-blend link that runs the helpful way. 'ceramides limit lipolysis by activating the PP2A-dependent dephosphorylation of HSL' (doi 10.3389/fphys.2022.826314). Acyl-CoAs made from released fat 'can further enter the ceramide-biosynthesis pathway'. ⇒ lowering ceramide releases this brake, which is a genuine mechanistic bridge to the Ceramide Blocker blend. Not a clinical claim; a mechanism. doi 10.3389/fphys.2022.826314
What it drives
It reduces Fat-releasing enzyme (HSL).
The true off-switch. 'Strictly speaking, cAMP degradation and PKA inactivation do not per SE terminate the lipolytic cascade. Lipolysis cessation ultimately depends on the dephosphorylation of PKA targets such as HSL and perilipin by protein phosphatases' (doi 10.3389/fphys.2022.826314). Measured: 'overexpression of the PP2A regulatory subunit B (B56-alpha) significantly decreased HSL Ser660 phosphorylation... while the knockdown of B56-alpha enhanced hormone-stimulated HSL activation and lipolysis.'. doi 10.3389/fphys.2022.826314
It reduces Releases stored fat.
'elevated b56-alpha/pp2a levels inhibit HSL activity and lipolysis, a possible mechanism underlying impaired adipose lipolysis in a high-fat diet-induced obese mouse model' (doi 10.3389/fphys.2022.826314). Recorded honestly: the same source says PP1, pp2a and pp2c 'all have a significant activity against HSL' and that 'additional research is needed to further pinpoint the specific phosphatase'. doi 10.3389/fphys.2022.826314
Blends that modulate it
Each blend page names this pathway and carries the study behind its claim.
See it on the map
Open the causal map to follow this pathway upstream and downstream, arrow by arrow, each with its study.