NR ASLN
AU Stuermer,C.A.O.; Langhorst,M.F.; Wiechers,M.F.; Legler,D.F.; von Hanwehr,S.H.; Guse,A.H.; Plattner,H.
TI PrPc capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction
QU The FASEB Journal 2004 Nov; 18(14): 1731-3
PT journal article
AB The cellular prion protein (PrPc) resides in lipid rafts, yet the type of raft and the physiological function of PrPc are unclear. We show here that cross-linking of PrPc with specific antibodies leads to 1) PrPc 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 Ca2+ 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 PrPc together with the reggies into limp-2 positive lysosomes. Thus, PrPc association with reggie rafts triggers distinct transmembrane signal transduction events in T cells that promote the focal concentration of PrPc itself by guiding activated PrPc into preformed reggie caps and then to the recruitment of important interacting signaling molecules.
MH Calcium Signaling; Cells, Cultured; Humans; Immunologic Capping; Jurkat Cells; Lysosomes/metabolism; MAP Kinase Signaling System; Membrane Microdomains/chemistry/*metabolism; Membrane Proteins/analysis/*metabolism; PrPc Proteins/analysis/immunology/*metabolism; Protein Transport; Research Support, Non-U.S. Gov't; *Signal Transduction; T-Lymphocytes/chemistry/enzymology/*metabolism
AD Department of Biology; University of Konstanz, 78457 Konstanz, Germany. Claudia.Stuermer@uni-konstanz.de
SP englisch
PO USA