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Mapping Perilipin 5 interactions via Protein Crosslinking Studies
Author(s) -
Forney Nathan B,
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.490.4
Subject(s) - perilipin , lipid droplet , lipid metabolism , chemistry , biochemistry , microbiology and biotechnology , biology , lipolysis , adipose tissue
Many human health issues in the United States are related to lipid metabolism, heart disease, obesity, type II diabetes, and non‐alcoholic fatty liver disease among them. Nearly all cells store neutral lipids in lipid storage droplets. Perilipins are a family of proteins known to associate with these lipid droplets. In particular, perilipin 5 is more strongly expressed in highly oxidative tissues such as cardiac tissues and fasting liver. Previously, we have identified a cytosolic pool of perilipin 5 which exists on small, lipoprotein‐like lipid droplets. Based on that work we hypothesized that quantification of perilipin 5 on these lipid droplets could identify interaction partners and help provide clues to perilipin function. To test this, cells expressing perilipin 5 are disrupted and lipid droplets are isolated. Bis[sulfosuccinimidyl] suberate (BS3) is used to crosslink proteins on these microdroplets. These cross‐linked proteins can then be separated by SDS‐PAGE and proteins crosslinked to perilipin 5 identified by western blotting. Overall, this data will allow for identification of perilipin 5 interaction partners on these structures and help identify if perilipin 5 acts as a monomer or multimer on lipid droplets. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .