Publikation: Cellular roles of the prion protein in association with reggie / flotillin microdomains
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2010
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Frontiers in bioscience. 2010, 15(3), pp. 1075-1085. ISSN 1093-9946. eISSN 1093-4715. Available under: doi: 10.2741/3662
Zusammenfassung
The prion protein (PrP) has been implicated in many diverse functions, making it difficult to pinpoint its basic physiological role. Our most recent studies in zebrafish, mammalian and invertebrate cells indicate that PrP regulates cell-cell communication, as well cell-matrix interactions at focal adhesions. In addition, we previously have shown that upon antibody-mediated cross-linking, PrP can be induced to cluster in the preformed T-cell cap. Here we review these data and discuss how the spatial link between PrP and the microdomain-forming proteins reggie- 1 (flotillin-2) and reggie-2 (flotillin-1) may contribute to PrP signaling, leading to the local assembly of membrane protein complexes at sites involved in cellular communication, such as cell-cell contacts, focal adhesions, the T-cell cap, and synapses.
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570 Biowissenschaften, Biologie
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SOLIS, Gonzalo P., Edward MÁLAGA-TRILLO, Helmut PLATTNER, Claudia STÜRMER, 2010. Cellular roles of the prion protein in association with reggie / flotillin microdomains. In: Frontiers in bioscience. 2010, 15(3), pp. 1075-1085. ISSN 1093-9946. eISSN 1093-4715. Available under: doi: 10.2741/3662BibTex
@article{Solis2010Cellu-8522,
year={2010},
doi={10.2741/3662},
title={Cellular roles of the prion protein in association with reggie / flotillin microdomains},
number={3},
volume={15},
issn={1093-9946},
journal={Frontiers in bioscience},
pages={1075--1085},
author={Solis, Gonzalo P. and Málaga-Trillo, Edward and Plattner, Helmut and Stürmer, Claudia}
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<dcterms:abstract xml:lang="eng">The prion protein (PrP) has been implicated in many diverse functions, making it difficult to pinpoint its basic physiological role. Our most recent studies in zebrafish, mammalian and invertebrate cells indicate that PrP regulates cell-cell communication, as well cell-matrix interactions at focal adhesions. In addition, we previously have shown that upon antibody-mediated cross-linking, PrP can be induced to cluster in the preformed T-cell cap. Here we review these data and discuss how the spatial link between PrP and the microdomain-forming proteins reggie- 1 (flotillin-2) and reggie-2 (flotillin-1) may contribute to PrP signaling, leading to the local assembly of membrane protein complexes at sites involved in cellular communication, such as cell-cell contacts, focal adhesions, the T-cell cap, and synapses.</dcterms:abstract>
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<dcterms:bibliographicCitation>First publ. in: Frontiers in bioscience 15 (2010), 3, pp. 1075-1085</dcterms:bibliographicCitation>
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