Gelsolin, an actin binding protein, regulates the actin cytoskeleton. Flightless I (fliI), a member of the gelsolin family, was discovered as a mutation in Drosophila that results in flightlessness and, in some cases, lethality. FliI is required for actin organization during myogenesis and embryogenesis. It contains characteristic gelsolin 6-fold segmental repeats and an N-terminal extension of 16 tandem leucine-rich repeats (LRR), which are involved in protein-protein interactions. The human flightless I (FLI) locus lies in a chromosomal region that is deleted in Smith-Magenis syndrome. The C-terminal region of FLI is 31% identical and 52% similar to human gelsolin. An attempt to detect an interaction between FLI and actin resulted in the discovery of FLI LRR Associated Protein (FLAP). FLAP is rich in α-helices and consists of central and C-terminal segments of dimeric coiled coils that are thought to mediate its interaction with FLI LRR. Therefore, FLAP appears to be part of the membrane cytoskeleton and serves as a binding ligand for LRR. This interaction implicates FLI as a linkage between the cytoskeleton and an unidentified intracellular structure.
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1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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