Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins

Abstract

The PAT family of proteins has been identified in eukaryotic species as diverse as vertebrates, insects, and amebazoa. These proteins share a highly conserved sequence organization and avidity for the surfaces of intracellular, neutral lipid storage droplets. The current nomenclature of the various members lacks consistency and precision, deriving more from historic context than from recognition of evolutionary relationship and shared function. In consultation with the Mouse Genomic Nomenclature Committee, the Human Genome Organization Genomic Nomenclature Committee, and conferees at the 2007 FASEB Conference on Lipid Droplets: Metabolic Consequences of the Storage of Neutral Lipids, we have established a unifying nomenclature for the gene and protein family members. Each gene member will incorporate the root term PERILIPIN (PLIN), the founding gene of the PAT family, with the different genes/proteins numbered sequentially.

C1q/Tumor Necrosis Factor-related Protein 11 (CTRP11), a Novel Adipose Stroma-derived Regulator of Adipogenesis

“…Ectopic expression of CTRP11 in 3T3-L1 cells inhibited adipocyte differentiation by suppressing the expression of PPAR-␥ and C/EBP-␣, two critical transcriptional regulators of adipogenesis (36 -38), and genes involved in lipid droplet metabolism and formation (i.e. perilipins) (42). The potential paracrine action of CTRP11 on adipocyte differentiation was confirmed by treating 3T3-L1 adipocytes with conditioned medium containing CTRP11 or purified recombinant protein.…”

Not Just Fat: The Structure and Function of the Lipid Droplet

“…PAT was named after perilipin, ADRP (also called adipophilin, ADFP), and tail-interacting protein of 47 kDa (TIP47), which were proposed to be renamed as PLIN1, PLIN2, and PLIN3 (Kimmel et al 2010). Together with S3-12 (PLIN4) and OXPAT/MLDP/LSDP5 (PLIN5), they constitute the PAT protein family.…”

Lipid droplet-associated PAT-proteins show frequent and differential expression in neoplastic steatogenesis

“…10 Lipid droplets exist in virtually any kind of normal cell and consist of a triacylglycerol core with a phospholipid monolayer on the surface in which amphiphilic proteins insert. These lipid dropletassociated proteins, such as perilipin, 11 adipophilin ('adipocyte-differentiation-related protein'), [12][13] and TIP47 ('tail-interacting protein of 47 kDa'), 14 subsumed as the PAT-family of proteins, and recently redefined as perilipin 1, perilipin 2, and perilipin 3, 15 are crucial for the formation, maintenance, modification, and involution of lipid droplets. Gene knockout experiments showed impaired lipid droplet function in certain cellular compartments, such as aberrant adipocyte lipolysis in perilipin-deficient mice [16][17] and protection against hepatic accumulation of lipid droplets but unimpaired adipogenesis in adipophilin-deficient mice.…”