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Papers In Press, published online ahead of print March 7, 2005
Biochemistry and Cell Biology, SUNY at Stony Brook, Stony Brook, NY 11794-5215
Corresponding Author: deborah.brown{at}sunysb.edu
Some transmembrane proteins must associate with lipid rafts to function. However, even if acylated, transmembrane proteins should not pack well with ordered raft lipids, and raft targeting is puzzling. Acylation is necessary for raft targeting of LAT. To determine whether an acylated transmembrane domain is sufficient, we examined raft association of palmitoylated and non-palmitoylated LAT transmembrane peptides in lipid vesicles by a fluorescence quenching assay, by microscopic examination, and by association with detergent-resistant membranes (DRMs). All three assays detected very low raft association of the non-acylated LAT peptide. DRM-association was the same as a control random transmembrane peptide. Acylation did not measurably enhance raft association by the first two assays, but slightly enhanced DRM association. The palmitoylated LAT peptide and a FLAG-tagged LAT transmembrane domain construct expressed in cells showed similar DRM association when both were reconstituted into mixed vesicles (containing cell-derived proteins and lipids and excess artificial raft-forming lipids) before detergent extraction. We conclude that the acylated LAT transmembrane domain has low inherent raft affinity. Full-length LAT in mixed vesicles associated better with DRMs than the peptide. However, cells appeared to contain two pools of LAT, with very different DRM affinities. As some LAT (but not the transmembrane domain construct) was isolated in a protein complex, and myc- and FLAG-tagged forms of LAT could be mutually co-immunoprecipitated, oligomerization or interactions with other proteins may enhance raft affinity of one pool of LAT. We conclude that both acylation and other factors, possibly protein-protein interactions, target LAT to rafts.
J. Biol. Chem, 10.1074/jbc.M500247200
Submitted on January 7, 2005
Revised on March 4, 2005
Accepted on March 7, 2005
Palmitoylation and intracellular-domain interactions both contribute to raft targeting of linker for activation of T cells (LAT)
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