The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha(7)beta(1) integrin receptor


Samson, T., Smyth, N., Janetzky, S., Wendler, O., Muller, J.M., Schule, R., Mark, H., Mark, K. and Wixler, V. (2004) The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha(7)beta(1) integrin receptor. Journal of Biological Chemistry, 279, (27), 28641-28652. (doi:10.1074/jbc.M312894200).

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Original Publication URL: http://dx.doi.org/10.1074/jbc.M312894200

Description/Abstract

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.

Item Type: Article
ISSNs: 0021-9258 (print)
Related URLs:
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56663
Date Deposited: 07 Aug 2008
Last Modified: 27 Mar 2014 18:39
URI: http://eprints.soton.ac.uk/id/eprint/56663

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