@article{Langhorst2008-04Traff-1191,
  year={2008},
  doi={10.1016/j.ejcb.2007.12.001},
  title={Trafficking of the microdomain scaffolding protein reggie-1/flotillin-2},
  number={4},
  volume={87},
  issn={0171-9335},
  journal={European Journal of Cell Biology},
  pages={211--226},
  author={Langhorst, Matthias F. and Reuter, Alexander and Jaeger, Friederike A. and Wippich, Frank M. and Luxenhofer, Georg and Plattner, Helmut and Stürmer, Claudia}
}

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    <dc:contributor>Stürmer, Claudia</dc:contributor>
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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T09:06:44Z</dc:date>
    <dc:creator>Langhorst, Matthias F.</dc:creator>
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    <dc:creator>Reuter, Alexander</dc:creator>
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    <dcterms:issued>2008-04</dcterms:issued>
    <dcterms:abstract xml:lang="eng">The reggie/flotillin proteins oligomerize and associate into clusters which form scaffolds for membrane microdomains. Besides their localization at the plasma membrane, the reggies/flotillins reside at various intracellular compartments; however, the trafficking pathways used by reggie-1/flotillin-2 remain unclear. Here, we show that trafficking of reggie-1/flotillin-2 is BFA sensitive and that deletion mutants of reggie-1/flotillin-2 accumulate in the Golgi complex in HeLa, Jurkat and PC12 cells, suggesting Golgi-dependent trafficking of reggie-1/flotillin-2. Using total internal reflection fluorescence microscopy, we observed fast cycling of reggie-1/flotillin-2-positive vesicles at the plasma membrane, which engaged in transient interactions with the plasma membrane only. Reggie-1/flotillin-2 cycling was independent of clathrin, but was inhibited by cholesterol depletion and microtubule disruption. Cycling of reggie-1/flotillin-2 was negatively correlated with cell cell contact formation but was stimulated by serum, epidermal growth factor and by cholesterol loading mediated by low density lipoproteins. However, reggie-1/flotillin-2 was neither involved in endocytosis of the epidermal growth factor itself nor in endocytosis of GPI-GFPs or the GPI-anchored cellular prion protein (PrPc). Reggie-2/flotillin-1 and stomatin-1 also exhibited cycling at the plasma membrane similar to reggie-1/flotillin-2, but these vesicles and microdomains only partially co-localized with reggie-2/flotillin-1. Thus, regulated vesicular cycling might be a general feature of SPFH protein-dependent trafficking.</dcterms:abstract>
    <dc:contributor>Langhorst, Matthias F.</dc:contributor>
    <dc:creator>Wippich, Frank M.</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/1191"/>
    <dc:contributor>Plattner, Helmut</dc:contributor>
    <dc:contributor>Luxenhofer, Georg</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: European Journal of Cell Biology ; 87 (2008), 4. - S. 211-226</dcterms:bibliographicCitation>
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    <dc:contributor>Wippich, Frank M.</dc:contributor>
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    <dc:creator>Luxenhofer, Georg</dc:creator>
    <dc:contributor>Jaeger, Friederike A.</dc:contributor>
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    <dcterms:title>Trafficking of the microdomain scaffolding protein reggie-1/flotillin-2</dcterms:title>
    <dc:creator>Stürmer, Claudia</dc:creator>
    <dc:language>eng</dc:language>
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    <dc:contributor>Reuter, Alexander</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T09:06:44Z</dcterms:available>
    <dc:creator>Plattner, Helmut</dc:creator>
    <dc:creator>Jaeger, Friederike A.</dc:creator>
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