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Linking membrane microdomains to the cytoskeleton: Regulation of the lateral mobility of reggie‐1/flotillin‐2 by interaction with actin
Author(s) -
Langhorst Matthias F.,
Solis Gonzalo P.,
Hannbeck Sylvia,
Plattner Helmut,
Stuermer Claudia A.O.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.074
Subject(s) - lipid microdomain , microbiology and biotechnology , actin , cytoskeleton , actin cytoskeleton , chemistry , mdia1 , lim domain , actin remodeling , biology , cell , membrane , biochemistry , gene , zinc finger , transcription factor
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.