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Characterization of the cytosolic pool of perilipin 5
Author(s) -
Brackbill James A,
Moeller Katherine,
Beussman Douglas J,
Tansey John T.
Publication year - 2013
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.27.1_supplement.588.4
Subject(s) - perilipin , cytosol , lipid droplet , immunoprecipitation , biochemistry , chemistry , proteome , intracellular , ultracentrifuge , microbiology and biotechnology , lipid metabolism , gel electrophoresis , biology , enzyme , lipolysis , adipose tissue , gene
The PAT family of lipid storage droplet (LD) associated proteins consists of five members, each an established regulator of neutral lipid metabolism. The most recently discovered family member, perilipin 5, has been shown to localize to two distinct intracellular pools: the lipid storage droplet and a cytosolic fraction, the nature of which is less understood. Characterization of the cytosolic fraction by way of sucrose gradient ultracentrifugation and non‐denaturing gel electrophoresis has indicated a density of 1.15 g/mL and a mass of 575 kDa for the particles on which LD‐dissociated perilipin 5 resides. The observed density and susceptibility of these structures to lipolytic degradation suggest that their core is rich in neutral lipid, much like the larger LD's. Based on the current understanding of these complexes, our lab is using a combination of immunoprecipitation and crosslinking techniques to identify other proteins that localize to these particles and interact with perilipin 5. Characterization of these candidate proteins holds the promise of yielding new insights into the regulation and function of the perilipin 5 protein, and to expand our understanding of lipid metabolism as a whole.