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J. Biol. Chem., Vol. 275, Issue 43, 33669-33678, October 27, 2000
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From the Institute for Biochemistry II, Medical Faculty, University
of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany
and § The Netherlands Cancer Institute,
Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
LIM proteins contain one or more double zinc
finger structures (LIM domains) mediating specific contacts between
proteins that participate in the formation of multiprotein complexes.
We report that the LIM-only protein DRAL/FHL2, with four and a half LIM
domains, can associate with
The LIM-only Protein DRAL/FHL2 Binds to the Cytoplasmic
Domain of Several
and 
Integrin Chains and Is Recruited to
Adhesion Complexes*
,
3A, 3B,
7A, and several 
integrin subunits as shown in yeast
two-hybrid assays as well as after overexpression in human cells. The
amino acid sequence immediately following the conserved
membrane-proximal region in the integrin subunits or the C-terminal
region with the conserved NXXY motif of the integrin subunits are critical for binding DRAL/FHL2. Furthermore, the DRAL/FHL2
associates with itself and with other molecules that bind to the
cytoplasmic domain of integrin subunits. Deletion analysis of
DRAL/FHL2 revealed that particular LIM domains or LIM domain
combinations bind the different proteins. These results, together with
the fact that full-length DRAL/FHL2 is found in cell adhesion
complexes, suggest that it is an adaptor/docking protein involved in
integrin signaling pathways.
*
This work was supported by the University of Cologne, the
Center National de la Recherche Scientifique (to M. A.), Deutsche Forschungsgemeinschaft Grants Kr 558/10-1, FOR265/2-1, SFB263, and AU
86/5-1, the Köln Fortune Program Numbers 160/1998 and 30/1999,
and the Dutch Cancer Society Grant NKI 95-979.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Institute for Experimental Medicine,
Friedrich-Alexander University, Glückstrasse 6, 91054 Erlangen, Germany.
¶
To whom correspondence should be addressed:
Institute for Biochemistry II, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany. Tel.: 49 221 478 6991; Fax: 49 221 478 3109; Email:
aumailley@uni-koeln.de.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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