Erin J. Cram
William H. Ahearn, Veronica S. Godoy-Carter
Date of Award
Master of Science
Department or Academic Unit
College of Arts and Sciences. Department of Biology.
C. elegans, filamin, biochemical, gene structure
Caenorhabditis elegans - Phylogeny, Genetic code, Biochemical genetics
Genetics and Genomics
Filamins are long, flexible, multi-domain proteins composed of an N-terminal actin-binding domain (ABD) followed by multiple immunoglobulin-like repeats (Ig-FLN). They function to anchor, organize and maintain the actin cytoskeleton, to provide scaffolds for signaling components, and to act as sensors for mechanical forces. In this study, we use a cDNA sequencing and bioinformatics approach to identify and describe the gene structure, expression patterns and phylogeny of the C. elegans filamin orthologs encoded by fln-1 and fln-2. We also used homology modeling to predict the protein structures. Our results reveal that C. elegans FLN-1 is well conserved at the sequence level with respect to vertebrate filamins, particularly in the ABD and several key Ig-FLN repeats. The domain organization of C. elegans FLN-1 is quite similar to filamins in humans and other organisms. FLN-2 is more divergent, with more than 23 Ig-FLN repeats interspersed among large regions that do not appear in other known filamins. Nevertheless, we demonstrated that FLN-2 binds actin and plays a role in cell attachment and cell migration in vivo. Knockdown by RNA interference of fln-2 results in defects in molting and cuticle attachment, tail morphogenesis, and distal tip cell (DTC) migration, which suggest that FLN-2 plays an important role in these processes. Our results help inform and validate future genetic and biochemical studies of filamin function, particularly those using C. elegans as a model system.
DeMaso, Christina, "Characterization of the gene structure and biochemical properties of the C. elegans filamin orthologs FLN-1 and FLN-2" (2010). Biology Master's Theses. Paper 14. http://hdl.handle.net/2047/d20000810
Click button above to open, or right-click to save.