[14] Concretely, beginning from the N-terminal of Perilipin-1, a PAT domain—characteristic of its protein family—can be found, followed by an also characteristic repeated sequence of 13 residues which form amphipathic helixes with an active role in linking membranes[15] and a 4-helix bundle before the C-terminal carbon.

[16] In Perilipin A, lipophile nature is conferred by the slightly hydrophobic amino acids concentrated in the central 25% of the sequence, region that anchors the protein to the core of the lipid droplet.

[17]Unlike its human ortholog, murine perilipin is composed of 517 amino acids in the primary structure of which several regions can be identified.

[19] Perilipin is a protein that coats lipid droplets (LDs) in adipocytes,[20] the fat-storing cells in adipose tissue.

[22] It handles essential functions in the regulation of basal and hormonally stimulated lipolysis[23] and also rises the formation of large LDs which implies an increase in the synthesis of triglycerides.

[21] In humans, Perilipin A is the most abundant protein associated with the adipocyte LDs[7] and lower PLIN1 expression is related with higher rates of lipolysis.

Then, Phosphorylated HSL translocates to the LD surface and associates with Perilipin A and Adipocyte fatty acid-binding protein (AFABP).

As a result, PKA phosphorylation implies an enriched colocation of HLS and ATGL which facilitates maximal lipolysis by the two lipases.

Even though perilipin-null mice present less fat mass and a higher insulin resistance, they do not show signs of a whole lipodystrophic phenotype.

[31] In humans, studies suggest that a deficiency of PLIN1 causes lipodystrophic syndromes,[32] which disables the optimal accumulation of triglycerides in adipocytes that derives in an abnormal deposition of lipids in tissues such as skeletal muscle and liver.

These findings affirm a new primary form of inherited lipodystrophy and emphasize on the severe metabolic consequences of a defect in the formation of lipid droplets in adipose tissue.