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Filamins are long, flexible, multi-domain proteins composed of an N-terminal actin-binding domain (ABD) followed by multiple immunoglobulin-like repeats (IgFLN). They function to organize and maintain the actin cytoskeleton, to provide scaffolds for signaling components, and to act as mechanical force sensors. In this study, we used transcript sequencing and homology modeling to characterize the gene and protein structures of the  C. elegans  filamin orthologs  fln-1  and  fln-2 . Our results reveal that  C. elegans  FLN-1 is well conserved at the sequence level to vertebrate filamins, particularly in the ABD and several key IgFLN repeats. Both FLN-1 and the more divergent FLN-2 colocalize with actin  in vivo . FLN-2 is poorly conserved, with at least 23 IgFLN repeats interrupted by large regions that appear to be nematode-specific. Our results indicate that many of the key features of vertebrate filamins are preserved in  C. elegans  FLN-1 and FLN-2, and suggest the nematode may be a very useful model system for further study of filamin function.

Structural and Functional Evaluation of C. elegans Filamins FLN-1 and FLN-2