PLIN5

Members of the perilipin family, such as PLIN5, coat intracellular lipid storage droplets and protect them from lipolytic degradation.

PERILIPIN 5

Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity).

Lipid droplet organizationISS:UniProtKB
Lipid storageManual Assertion Based On ExperimentIBA:GO_Central
Mitochondrion localizationIEA:Ensembl
Negative regulation of fatty acid beta-oxidationISS:UniProtKB
Negative regulation of lipase activityISS:UniProtKB
Negative regulation of peroxisome proliferator activated receptor signaling pathwayISS:UniProtKB
Negative regulation of reactive oxygen species metabolic processISS:UniProtKB
Negative regulation of triglyceride catabolic processISS:UniProtKB
Positive regulation of fatty acid beta-oxidationISS:UniProtKB
Positive regulation of lipase activityISS:UniProtKB
Positive regulation of lipid storageISS:UniProtKB
Positive regulation of sequestering of triglycerideISS:UniProtKB
Positive regulation of triglyceride biosynthetic processISS:UniProtKB

Lipid droplet
Cytoplasm
Mitochondrion
Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm.

Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle at rest or upon lipolytic stimulation (By similarity).