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Identification of a putative perilipin 5 splice variant (606.6)
Author(s) -
Hardy Cara,
DuBreuil Daniel,
Hubbell Theresa,
Tansey John
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.606.6
Subject(s) - perilipin , lipid droplet , microbiology and biotechnology , biology , lipid metabolism , chemistry , biochemistry , lipolysis , adipose tissue
Cells store neutral lipid in lipid storage droplets. These organelles have a coating of regulatory proteins including the perilipins, a family of related proteins which regulate and scaffold lipolytic enzymes. At least one of these proteins (perilipin 1) has been shown to have several truncated forms that arise through differential mRNA splicing. Using western blotting we have identified a truncated form of perilipin 5 we have termed perilipin 5B. This protein is found in murine tissue as well as cultured cells. Using RT‐PCR we have identified multiple amplicons suggesting that perilipin 5B contains a read through of intron 8 of the murine perilipin 5 gene. shRNA studies conducted in cultured cells result in decreased levels of the protein. In addition, immunofluorescence microscopy revealed that perilipin 5B is unable to bind to mature lipid droplets, but does form distinct puncta in the cytosol. Taken together, this data suggests that perilipin 5B is a splice variant of perilipin 5 found in oxidative tissues but is unable to bind to large lipid droplets. The role of this protein in neutral lipid metabolism remains unclear.