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PrP c capping in T cells promotes its association with the lipid raft proteins reggie‐1 and reggie‐2 and leads to signal transduction
Author(s) -
Stuermer Claudia A. O.,
Langhorst Matthias F.,
Wiechers Marianne F.,
Legler Daniel F.,
Hanwehr Sylvia Hannbeck von,
Guse Andreas H.,
Plattner Helmut
Publication year - 2004
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.04-2150fje
Subject(s) - lipid raft , microbiology and biotechnology , fyn , signal transduction , jurkat cells , internalization , phosphorylation , caveolae , biology , raft , chemistry , proto oncogene tyrosine protein kinase src , cell , t cell , immunology , biochemistry , polymer , immune system , organic chemistry , copolymer
The cellular prion protein (PrP c ) resides in lipid rafts, yet the type of raft and the physiological function of PrP c are unclear. We show here that cross‐linking of PrP c with specific antibodies leads to 1) PrP c capping in Jurkat and human peripheral blood T cells; 2) to cocapping with the intracellular lipid raft proteins reggie‐1 and reggie‐2; 3) to signal transduction as seen by MAP kinase phosphorylation and an elevation of the intracellular Ca 2+ concentration; 4) to the recruitment of Thy‐1, TCR/CD3, fyn, lck and LAT into the cap along with local tyrosine phosphorylation and F‐actin polymerization, and later, internalization of PrP c together with the reggies into limp‐2 positive lysosomes. Thus, PrP c association with reggie rafts triggers distinct transmembrane signal transduction events in T cells that promote the focal concentration of PrP c itself by guiding activated PrP c into preformed reggie caps and then to the recruitment of important interacting signaling molecules.