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http://purl.uniprot.org/citations/17854803 | http://www.w3.org/2000/01/rdf-schema#comment | "The reggies/flotillins are oligomeric scaffolding proteins for membrane microdomains. We show here that reggie-1/flotillin-2 microdomains are organized along cortical F-actin in several cell types. Interaction with F-actin is mediated by the SPFH domain as shown by in vivo co-localization and in vitro binding experiments. Reggie-1/flotillin-2 microdomains form independent of actin, but disruption or stabilization of the actin cytoskeleton modulate the lateral mobility of reggie-1/flotillin-2 as shown by FRAP. Furthermore, reggie/flotillin microdomains can efficiently be immobilized by actin polymerisation, while exchange of reggie-1/flotillin-2 molecules between microdomains is enhanced by actin disruption as shown by tracking of individual microdomains using TIRF microscopy."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2007.08.074"xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/author | "Plattner H."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/author | "Stuermer C.A."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/author | "Solis G.P."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/author | "Langhorst M.F."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/author | "Hannbeck S."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/name | "FEBS Lett"xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/pages | "4697-4703"xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/title | "Linking membrane microdomains to the cytoskeleton: regulation of the lateral mobility of reggie-1/flotillin-2 by interaction with actin."xsd:string |
http://purl.uniprot.org/citations/17854803 | http://purl.uniprot.org/core/volume | "581"xsd:string |
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