This protein group has been shown to be responsible for lipid droplet's biogenesis, structure and degradation.

[6] Inside the cell, PLIN5 can be found in multiple intracellular structures including lipid droplets, endoplasmic reticulum, mitochondria, and the cytosol.

This family began to split during the first and second vertebrate genome duplication,[9] giving birth to six types of PLIN genes, expressed throughout the animal kingdom.

[12] In addition, perilipin 5 regulates the activation of hepatic stellate cell, implicated in fibrosis, which is the creation of new tissue to repair the one damaged.

Perilipin 5 coats the lipid droplet acting as a barrier to triglyceride, thus increasing its storage.

When needed, perilipin 5 is phosphorylated by protein kinase A, which allows it to access the nucleus and enter the complex SIRT1/PGC-1α, involved in fatty acid oxidation.

[16] Higher levels of perilipin 5 are closely related to the association between lipid droplet and mitochondria.

On the other hand, this association may occur with the aim of protecting the mitochondria against toxic levels of fatty acids in the cytosol.

An increase in PLIN5 expression leads to the accumulation of triglyceride content and to the enlargement of LDs and a reduction in its number.

Despite massive steatosis, overexpression of cardiac PLIN5 is compatible with normal heart function and lifespan.

Medium and high concentrations of ROS can induce apoptosis and eventually cause necrosis through oxidative stress.

Mitochondria from hearts suffering from a Plin5 deficiency had a membrana whose fatty acyl composition was altered, and its depolarization was compromised.