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J. Biol. Chem., Vol. 279, Issue 27, 28641-28652, July 2, 2004

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The LIM-only Proteins FHL2 and FHL3 Interact with - and -Subunits of the Muscle ₇₁ Integrin Receptor^*

Thomas Samson, Neil Smyth, Stefanie Janetzky, Olaf Wendler, Judith M. Müller¶, Roland Schüle¶, Helga von der Mark, Klaus von der Mark, and Viktor Wixler||

From the Lehrstuhl für Experimentelle Medizin I, Nikolaus-Fiebiger Zentrum für Molekulare Medizin, Friedrich-Alexander Universität Erlangen/Nürnberg, Glückstrasse 6, 91054 Erlangen, Germany, Institut für Biochemie, Medizinische Fakultät der Universität zu Köln, Joseph-Stelzmann Strasse 52, 50931 Cologne, Germany, and ^¶Universitäts-Frauenklinik und Zentrum für Klinische Forschung, Klinikum der Universität Freiburg, Breisacherstrasse 66, 79106 Freiburg, Germany

FHL1, FHL2, and FHL3 are members of the four and one-half LIM domain protein subclass that are expressed in striated muscles. Here we show that FHL2 and FHL3 are novel ₇₁ integrin-interacting proteins. They bind both the - and the -subunit as well as different splice isoforms. The minimal binding sites for FHL2 and FHL3 on _1A-chain overlap, whereas on _7A and _7B 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 - or the -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 ₇₁ integrin receptor at the periphery of Z-discs, suggesting a role in mechanical stabilization of muscle cells.

Received for publication, November 25, 2003 , and in revised form, April 3, 2004.

^* This work was supported by Deutsche Forschungsgemeinschaft Grants DFG Wi 1235/4-1 (to V. W.), DFG Sm 65/1-2 (to N. S.), and DFG Ma 534/15-1 (to K. v. d. M.) and by Mildred-Scheel-Stiftung Grant 10-2019-Bu1 (to R. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence should be addressed. Tel.: 49-9131-852-9124; Fax: 49-9131-852-6341; E-mail: vwixler{at}molmed.uni-erlangen.de.

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