Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-2-22
pubmed:abstractText
Lateral mobility and spatial organization of proteins within the plasma membrane are likely to mediate the initial events coordinating T cell activation. Lipid rafts, distinct cholesterol/sphingolipid-rich membrane microdomains, provide a mechanism for this regulation by concentrating or excluding signaling proteins. We demonstrate in peripheral blood T cell lymphoblasts that immediate early phosphotyrosine signal transduction through the TCR complex is functionally dependent on a distinct population of lipid rafts. Specifically, cholesterol extraction destabilizes the membrane microdomains containing Lck, while the rafts containing the adapter protein linker for activation of T cells remain intact. Heterogeneity in the partitioning of these proteins in resting cells was confirmed by immunoelectron microscopy. After T cell activation, both Lck and the linker for activation of T cells colocalize to 50-100 nm microdomains in the plasma membrane, indicating that sequestration of these proteins into distinct lipid rafts may function to regulate the initiation of T cell signal transduction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, http://linkedlifedata.com/resource/pubmed/chemical/Cyclodextrins, http://linkedlifedata.com/resource/pubmed/chemical/LAT protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Specific Protein..., http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell, http://linkedlifedata.com/resource/pubmed/chemical/ZAP-70 Protein-Tyrosine Kinase, http://linkedlifedata.com/resource/pubmed/chemical/ZAP70 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/antigen T cell receptor, zeta chain, http://linkedlifedata.com/resource/pubmed/chemical/beta-Cyclodextrins, http://linkedlifedata.com/resource/pubmed/chemical/methyl-beta-cyclodextrin
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
168
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2233-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11859110-Adaptor Proteins, Signal Transducing, pubmed-meshheading:11859110-Antigens, CD4, pubmed-meshheading:11859110-Blood, pubmed-meshheading:11859110-Carrier Proteins, pubmed-meshheading:11859110-Cells, Cultured, pubmed-meshheading:11859110-Cholesterol, pubmed-meshheading:11859110-Cyclodextrins, pubmed-meshheading:11859110-Humans, pubmed-meshheading:11859110-Lymphocyte Activation, pubmed-meshheading:11859110-Lymphocyte Specific Protein Tyrosine Kinase p56(lck), pubmed-meshheading:11859110-Membrane Microdomains, pubmed-meshheading:11859110-Membrane Proteins, pubmed-meshheading:11859110-Phosphoproteins, pubmed-meshheading:11859110-Phosphorylation, pubmed-meshheading:11859110-Phosphotyrosine, pubmed-meshheading:11859110-Protein-Tyrosine Kinases, pubmed-meshheading:11859110-Receptors, Antigen, T-Cell, pubmed-meshheading:11859110-Signal Transduction, pubmed-meshheading:11859110-T-Lymphocytes, pubmed-meshheading:11859110-ZAP-70 Protein-Tyrosine Kinase, pubmed-meshheading:11859110-beta-Cyclodextrins
pubmed:year
2002
pubmed:articleTitle
Lipid raft heterogeneity in human peripheral blood T lymphoblasts: a mechanism for regulating the initiation of TCR signal transduction.
pubmed:affiliation
Department of Pathology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.