Premium
Docosahexaenoic acid selectively inhibits plasma membrane targeting of lipidated proteins
Author(s) -
Seo Jeongmin,
Barhoumi Rola,
Johnson Arthur E.,
Lupton Joanne R.,
Chapkin Robert S.
Publication year - 2006
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/fj.05-4683fje
Subject(s) - endomembrane system , microbiology and biotechnology , cytosol , docosahexaenoic acid , membrane , membrane protein , green fluorescent protein , cell membrane , biochemistry , cytoplasm , chemistry , biology , polyunsaturated fatty acid , fatty acid , vesicle , gene , enzyme
ABSTRACT Membrane localization of lipidated cytosolic signaling proteins is mediated by interactions between specific lipid anchors and membranes, but little is known about the regulatory role of membrane composition in lipidated protein membrane targeting. Here, using green fluorescent protein (GFP) chimeras and quantitative fluorescence microscopy in living mouse colonocytes, we show that docosahexaenoic acid (DHA), a dietary polyunsaturated fatty acid (PUFA) with membrane lipid‐modifying properties, selectively inhibits plasma membrane (PM) targeting and increases the endomembrane localization of lipidated proteins that are cytoplasmic cargo in the exocytic pathway, without affecting the exocytic pathway itself. DHA selectivity seems to be dictated by the protein trafficking route, independent of the functional state of proteins and the location and composition of membrane anchors. DHA enrichment in cell membranes was required to elicit the inhibitory effect. These data reveal that membrane lipid composition influences cell signaling by modulating intracellular trafficking and localization of membrane proteins, providing a potential molecular mechanism for the documented health benefits of DHA.