Abstract
Hydrophobic and electrostatic interactions anchor perilipin 2 to the surface of cytosolic lipid droplets
The FASEB journal, Vol.26(S1), pp.594.4-594.4
04/2012
DOI: 10.1096/fasebj.26.1_supplement.594.4
Abstract
Abstract only All eukaryotic organisms store excess lipid in intracellular lipid droplets. These dynamic structures are associated with and regulated by numerous proteins. One such protein, perilipin 2, is present on lipid droplets in most lipid storing cells. However, the mechanism by which perilipin 2 localizes and remains anchored to the lipid droplet surface is unknown. The objective of our study was to determine the roles of hydrophobic and electrostatic interactions in perilipin 2 localization. Lipid droplets coated with perilipin 2 were incubated with reagents designed to disrupt either electrostatic or hydrophobic interactions. We show that disrupting hydrophobic interactions, between proteins and surface phospholipids, causes perilipin 2 to dissociate from the lipid droplet. Unexpectedly, disturbing electrostatic attractions between perilipin 2 and surface phospholipids also compromised binding. Future studies aim to identify the specific characteristics of the lipid droplet surface that mediate the binding of perilipin 2 and other lipid droplet proteins. This work was funded by the Research Corporation for Science Advancement (LL) and through the generous support of Dr. Elizabeth Nabel (ACS).
Details
- Title: Subtitle
- Hydrophobic and electrostatic interactions anchor perilipin 2 to the surface of cytosolic lipid droplets
- Creators
- Arthur C. Sletten - St. Olaf CollegeAlison E. Seline - St. Olaf CollegeLaura L. Listenberger - St. Olaf College
- Resource Type
- Abstract
- Publication Details
- The FASEB journal, Vol.26(S1), pp.594.4-594.4
- DOI
- 10.1096/fasebj.26.1_supplement.594.4
- ISSN
- 0892-6638
- eISSN
- 1530-6860
- Language
- English
- Date published
- 04/2012
- Academic Unit
- Pathology; Dermatology
- Record Identifier
- 9984642495102771
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