PrPc capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction : [Langfassung]

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102_HrPc_capping_in_T_cells.pdf
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2004
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Langhorst, Matthias F.
Hannbeck von Hanwehr, Sylvia
Guse, Andreas H.
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The FASEB Journal. 2004, 18(14), pp. 1731-1733. ISSN 0892-6638. eISSN 1530-6860. Available under: doi: 10.1096/fj.04-2150fje
Zusammenfassung

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.

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570 Biowissenschaften, Biologie
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noncaveolar microdomains, reggie/flotillin, PrPc cross-linking
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ISO 690STÜRMER, Claudia, Matthias F. LANGHORST, Marianne F. WIECHERS, Daniel F. LEGLER, Sylvia HANNBECK VON HANWEHR, Andreas H. GUSE, Helmut PLATTNER, 2004. PrPc capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction : [Langfassung]. In: The FASEB Journal. 2004, 18(14), pp. 1731-1733. ISSN 0892-6638. eISSN 1530-6860. Available under: doi: 10.1096/fj.04-2150fje
BibTex
@article{Sturmer2004-11cappi-8817,
  year={2004},
  doi={10.1096/fj.04-2150fje},
  title={PrPc capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction : [Langfassung]},
  number={14},
  volume={18},
  issn={0892-6638},
  journal={The FASEB Journal},
  pages={1731--1733},
  author={Stürmer, Claudia and Langhorst, Matthias F. and Wiechers, Marianne F. and Legler, Daniel F. and Hannbeck von Hanwehr, Sylvia and Guse, Andreas H. and Plattner, Helmut},
  note={"published ahead of print September 2, 2004"  - deswegen ohne Seitenzahlen}
}
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    <dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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"published ahead of print September 2, 2004" - deswegen ohne Seitenzahlen
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