The murine perilipin gene: the lipid droplet-associated perilipins derive from tissue-specific, mRNA splice variants and define a gene family of ancient origin
Xy. Lu et al., The murine perilipin gene: the lipid droplet-associated perilipins derive from tissue-specific, mRNA splice variants and define a gene family of ancient origin, MAMM GENOME, 12(9), 2001, pp. 741-749
The Perilipins are a family of intracellular neutral lipid droplet storage
proteins that are responsive to acute protein kinase A-mediated, hormonal s
timulation. Perilipin (Peri) expression appears to be limited to adipocytes
and steroidogenic cells, in which intracellular neutral lipid hydrolysis i
s regulated by protein kinase A. We have isolated cDNA sets and overlapping
genomic fragments of the murine Peri locus and mapped chromosomal location
, transcription start sites, polyadenylylation sites, and intron/exon junct
ions. Data confirm that the Perilipins are encoded by a single-copy gene, w
ith alternative and tissue-specific, mRNA splicing and polyadenylylation yi
elding four different protein species. The Perilipin proteins have identica
l similar to 22-kDa amino termini with distinct carboxyl terminal sequences
of varying lengths. These genomic and transcriptional maps of murine. Peri
lipin are also essential for evaluating presumptive endogenous and targeted
mutations within the locus. The N-terminal identity region of the Perilipi
ns defines a sequence motif, which we term PAT, that is shared with the ADR
P and TIP47 proteins; additionally, the PAT domain may represent a novel, c
onserved pattern for lipid storage droplet (LSD) proteins of vertebrates an
d invertebrates alike. Comparative genomics suggest the presence of related
LSD genes in species as diverse as Drosophila and Dictyostelium.