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Interaction of Perilipin 5 with Mitochondria
Author(s) -
Todd Claire I,
Tansey John T
Publication year - 2019
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.2019.33.1_supplement.490.16
Subject(s) - perilipin , lipid droplet , microbiology and biotechnology , mitochondrion , population , lipid metabolism , biology , cytosol , chemistry , biochemistry , lipolysis , adipose tissue , medicine , enzyme , environmental health
Problems with lipid metabolism can lead to array of diseases such as fatty liver disease, obesity, and diabetes. Nearly one‐third of the world's population is obese or overweight, and struggle with these diseases. Cellular lipids are found in lipid storage droplets. Perilipins are a family of proteins that associate with the surface of lipid storage droplets and regulate their contents. We used CHO cells expressing perilipin 5 protein and assayed them using immunofluorescent microscopy to determine if mitochondria interact with perilipin 5 under different phosphorylation states. We hypothesized that the interaction of mitochondria and perilipin 5 was phosphorylation dependent. We used antibodies that detect either FLAG tagged and native perilipin 5 and Mitotracker red to stain cells and forskolin and IBMX to activate the PKA signaling pathway. Following one hour of stimulation, perilipin 5 appeared in the lipid droplets and cytosol of the cell but interactions with mitochondria were not apparent. In this model 3 hours of stimulation is required for perilipin 5 to translocate to the nucleus. Collectively these ongoing studies show that the cellular partitioning of perilipin 5 is in part phosphorylation dependent. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .