Linked Life Data

15753089

Source:http://linkedlifedata.com/resource/pubmed/id/15753089

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2005-5-9
pubmed:abstractText
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 linker for activation of T cells (LAT). To determine whether an acylated transmembrane domain is sufficient, we examined raft association of palmitoylated and nonpalmitoylated 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 nonacylated 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 raft affinities. Since some LAT (but not the transmembrane domain construct) was isolated in a protein complex, and the 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18931-42
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15753089-Animals, pubmed-meshheading:15753089-COS Cells, pubmed-meshheading:15753089-Detergents, pubmed-meshheading:15753089-Dose-Response Relationship, Drug, pubmed-meshheading:15753089-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15753089-Fluorescent Dyes, pubmed-meshheading:15753089-Humans, pubmed-meshheading:15753089-Immunoprecipitation, pubmed-meshheading:15753089-Jurkat Cells, pubmed-meshheading:15753089-Lipids, pubmed-meshheading:15753089-Lymphocyte Activation, pubmed-meshheading:15753089-Membrane Microdomains, pubmed-meshheading:15753089-Octoxynol, pubmed-meshheading:15753089-Palmitic Acid, pubmed-meshheading:15753089-Peptides, pubmed-meshheading:15753089-Plasmids, pubmed-meshheading:15753089-Protein Binding, pubmed-meshheading:15753089-Protein Structure, Tertiary, pubmed-meshheading:15753089-Rhodamines, pubmed-meshheading:15753089-Spectrometry, Fluorescence, pubmed-meshheading:15753089-T-Lymphocytes, pubmed-meshheading:15753089-Temperature
pubmed:year
2005
pubmed:articleTitle
Palmitoylation and intracellular domain interactions both contribute to raft targeting of linker for activation of T cells.
pubmed:affiliation
Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural