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

The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha(7)beta(1) integrin receptor
The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha(7)beta(1) integrin receptor
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.
0021-9258
28641-28652
Samson, T.
5579aa0b-6a1e-4ac3-9004-9bb75d6ad097
Smyth, N.
0eba2a40-3b43-4d40-bb64-621bd7e9d505
Janetzky, S.
cc8bded1-7dd1-42af-b740-f8c9742c54ba
Wendler, O.
1bb4267d-c06f-436c-9b05-52e164172679
Muller, J.M.
72695286-d90f-4f54-845e-34332dc56134
Schule, R.
8aa1a4a4-5c10-4cb9-8d0a-7a5f8c7381e6
Mark, H.
67a49ae7-470c-497a-a592-2b61f35216ee
Mark, K.
cc301c94-d687-412d-9394-d2a7c28f4f59
Wixler, V.
7b3c69d6-78ff-4e5b-b590-d3e6c246622d
Samson, T.
5579aa0b-6a1e-4ac3-9004-9bb75d6ad097
Smyth, N.
0eba2a40-3b43-4d40-bb64-621bd7e9d505
Janetzky, S.
cc8bded1-7dd1-42af-b740-f8c9742c54ba
Wendler, O.
1bb4267d-c06f-436c-9b05-52e164172679
Muller, J.M.
72695286-d90f-4f54-845e-34332dc56134
Schule, R.
8aa1a4a4-5c10-4cb9-8d0a-7a5f8c7381e6
Mark, H.
67a49ae7-470c-497a-a592-2b61f35216ee
Mark, K.
cc301c94-d687-412d-9394-d2a7c28f4f59
Wixler, V.
7b3c69d6-78ff-4e5b-b590-d3e6c246622d

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. The Journal of Biological Chemistry, 279 (27), 28641-28652. (doi:10.1074/jbc.M312894200).

Record type: Article

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.

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Published date: 1 July 2004

Identifiers

Local EPrints ID: 56663
URI: http://eprints.soton.ac.uk/id/eprint/56663
ISSN: 0021-9258
PURE UUID: ee81c112-703d-42dd-9444-7297aaeec460

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Date deposited: 07 Aug 2008
Last modified: 08 Jan 2022 16:02

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Contributors

Author: T. Samson
Author: N. Smyth
Author: S. Janetzky
Author: O. Wendler
Author: J.M. Muller
Author: R. Schule
Author: H. Mark
Author: K. Mark
Author: V. Wixler

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