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.


Originally published in PLoS ONE 6(7): e22428. 2011. doi:10.1371/journal.pone.0022428

National Institutes of Health (NIH) R01 GM85077 to E.J. Cram partially supported this study (www.nih.gov). Other funding came from internal startup funds provided by Northeastern University, Boston, Massachusetts. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.


C. elegans, filamins, gene structures, protein structures

Subject Categories

Caenorhabditis elegans - Genetics


Cell Biology | Genetics


Public Library of Science

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Copyright 2011. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Christina R. DeMaso, Ismar Kovacevic, Alper Uzun, Erin J. Cram

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