Triglyceride assembly
You want it quiet during release. In fasting humans roughly forty percent of what is released is returned this way. And the cruellest detail is a candidate, nOT a certainty: this enzyme can be phosphorylated by the same kinase that starts release, so the accelerator may be turning the handbrake. The source that proposes it uses the word might, and so do we.
In depth
The enzyme that takes released fat and puts it straight back into the droplet.
What drives it
Lipolysis signal increases it.
The accelerator may be turning the handbrake. 'it has been reported that DGAT1 can be phosphorylated by PKA-dependent pathway. Therefore, PKA might phosphorylatE and activate DGAT1 during lipolysis to promote reesterification' (doi 10.3389/fphys.2022.826314). 'might' is the source's word and it is kept. This is the candidate mechanism for why putting-back rises with letting-out. doi 10.3389/fphys.2022.826314
Fat-releasing enzyme (ATGL) increases it.
The futile cycle is structural, not incidental — and the Russian literature puts a harder number on it than the English. 'Базальный распад и синтез триацилглицеролов в жировой ткани объединены в СУБСТРАТНЫЙ ЦИКЛ... 1,3-ДАГ, продукт малоактивной ATGL, является ПРЕДПОЧТИТЕЛЬНЫМ СУБСТРАТОМ одного из ферментов синтеза триацилглицеролов – ДАГ-ацил-трансферазы. В результате ATGL и ДАГ-ацил-ТФ действуют СКООРДИНИРОВАННО и поддерживают НЕПРЕРЫВНЫЙ ЦИКЛ ГИДРОЛИЗА-РЕЭТЕРИФИКАЦИИ ТАГ' = the product of the rate-limiting lipase is the preferred substrate of the re-esterifying enzyme; the two ACT in coordination and maintain a continuous hydrolysis-re-esterification cycle (biokhimija.ru/biokhimiya-zhirovoj-tkani/lipoliz.html (русский)). The rate: 'В состоянии покоя около 70% жирных кислот, высвобожденных при участии малоактивной ATGL, НЕ ПОКИДАЮТ КЛЕТКУ и включаются обратно в состав ТАГ' = at rest, about 70% of the fatty acids released do not leave the cell and ARE put back into triglyceride. The English literature gives ~40% for this. The Russian figure is 70% and it is specifically for the basal, low-activity state. Sources: PMID 23066022; PMC3510842. doi 10.1074/jbc.M112.400416. · PMID 23066022 · PMC3510842
What it drives
It increases Fat re-storage.
10.1016/j.molmet.2022.101499 — 10.21748/lipidlibrary.39186 — The named enzyme that performs the return. Same source: dag-acyltransferase takes 1,3-dag straight back to triglyceride, and it prefers the lipase's own product, so the return arm is fed by the release arm (biokhimija.ru/biokhimiya-zhirovoj-tkani/lipoliz.html (русский)). This is why inhibiting that enzyme is a different and arguably better place to stand than pushing release harder: it removes the arm that is recapturing most of what was just released. doi 10.1016/j.molmet.2022.101499
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.