Membrane compartmentation and the response to antigen

Current Opinion in Immunology

Volumn 11, Issue 3, 1999, Pages 265-269

  Xavier, Ramnik ^a  

^a MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; MEMBRANE LIPID; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; T LYMPHOCYTE RECEPTOR;

ANTIGEN RECOGNITION; CYTOSKELETON; HUMAN; LYMPHOCYTE MEMBRANE; MEMBRANE STRUCTURE; PROTEIN DOMAIN; SHORT SURVEY; SIGNAL TRANSDUCTION; T LYMPHOCYTE; T LYMPHOCYTE ACTIVATION;

EID: 0032986671     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(99)80043-0     Document Type: Article

References (5)

1. Stefanova I, Horejsi V, Ansotegui U, Knapp W, Stockinger H: GPI-anchored cell-surface molecules complexed to protein tyrosine Kinases. Science 1991, 254:1016-1019.
2. Brown DA, Rose JK: Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68:533-544.
3. Simons K, Ikonen E: Functional rafts in cell membranes. Nature 1997, 387:569-572.
4. Friedrichson T, Kurzchalia TV: Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 1998, 394:802-805.
5. Varma R, Mayor S: GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 1998, 394:798-801. In these two studies [4,5], FRET (fluorescence-resonant-energy transfer) and chemical crosslinking are used to demonstrate that lipid microdomains are dynamic structures in living cells and that glycosyl phosphatidylinositol (GPI)-linked molecules reside in these 70 nm compartments.