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Papers In Press, published online ahead of print April 26, 2004
Lehrstuhl für Experimentelle Medizin I, Friedrich-Alexander Universität Erlangen/Nuernberg, Erlangen 91054
Corresponding Author: vwixler{at}molmed.uni-erlangen.de
FHL1, FHL2 and FHL3 are members of the four and half LIM domain protein subclass that are expressed in striated muscles. Here we show that FHL2 and FHL3 are novel a7ß1 integrin interacting proteins. They bind both the a- and the ß-subunit as well as different splice isoforms. The minimal binding sites for FHL2 and FHL3 on ß1A-chain overlap, whereas on a7A and a7B subunits they are situated adjacent. Determining the binding sites for integrins on FHL2 or FHL3 revealed that the suprastructure of the whole molecule is important for these associations, rather than any single LIM domain. Immunofluorescence studies with cells expressing full-length FHL proteins or their deletion mutants showed that FHL2 and FHL3 but not FHL1 colocalize with integrins at cell adhesion sites. Further, their recruitment to the membrane results from binding to either the a- or the ß-chain of the integrin receptor. The association of FHL2 or FHL3 with integrin receptors neither influences attachment of cells to different substrates nor changes their migration capacity. However, in cardiac and skeletal muscles FHL2 and FHL3, respectively, are colocalized with a7ß1 integrin receptor at the periphery of Z-discs suggesting a role in mechanical stabilization of muscle cells.
J. Biol. Chem, 10.1074/jbc.M312894200
Submitted on November 25, 2003
Revised on April 26, 2004
Accepted on April 26, 2004
The LIM-only proteins FHL2 and FHL3 interact with
- and 
-subunits of the muscle 71 integrin receptor
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