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Papers In Press, published online ahead of print April 18, 2003
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3168
Corresponding Author: christina.mitchell{at}med.monash.edu.au
Four and a half LIM domain (FHL) proteins are members of the LIM protein super family. Several FHL proteins function as co-activators of CREM/CREB transcription factors and the androgen receptor. FHL3 is highly expressed in skeletal muscle, but its function is unknown. FHL3 localized to the nucleus in C2C12 myoblasts, and following integrin engagement, exited the nucleus and localized to actin stress fibers and focal adhesions. In mature skeletal muscle FHL3 was found at the Z-line. Actin was identified as a potential FHL3 binding partner in yeast-two-hybrid screening of a skeletal muscle library. FHL3 complexed with actin both in vitro and in vivo as shown by GST-pull-down assays and co-immunoprecipition of recombinant and endogenous proteins. FHL3 promoted cell spreading and when over expressed in spread C2C12 cells disrupted actin stress fibers. Increased FHL3 expression was detected in highly motile cells migrating into an artificial wound, compared to non-motile cells. The molecular mechanism by which FHL3 induced actin stress fiber disassembly was demonstrated by low speed actin co-sedimentation assays and electron microscopy. FHL3 inhibited
J. Biol. Chem, 10.1074/jbc.M213259200
Submitted on December 30, 2002
Revised on March 20, 2003
Accepted on April 17, 2003
FHL3 is an actin-binding protein that regulates alpha-actinin mediated actin bundling. FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly
-actinin mediated actin bundling. These studies reveal FHL3 as a significant regulator of actin cytoskeletal dynamics in skeletal myoblasts.
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