Identification of the binding partners for flightless I, A novel protein bridging the leucine-rich repeat and the gelsolin superfamilies.

The Journal of Biological Chemistry
Y T Liu, H L Yin

Abstract

Flightless-I (fliI) is a novel member of the gelsolin family that is important for actin organization during Drosophila embryogenesis and myogenesis. Drosophila fliI and the human homolog FLI both contain the classic gelsolin 6-fold segmental repeats and an amino-terminal extension of 16 tandem leucine-rich repeats (LRR). LRR repeats form amphipathic beta-alpha structural units that mediate protein-protein interactions. Although there are close to 100 known LRR domain-containing proteins, only a few binding pairs have been identified. In this paper, we used biochemical and genetic approaches to identify proteins that interact with human FLI. In vitro synthesized FLI bound to actin-Sepharose and binding was reduced by competition with excess soluble actin. Actin binding was mediated through the gelsolin-like domain and not the LRR domain. Although the FLI LRR module is most closely related to the LRR domains of Ras-interactive proteins, FLI does not associate with Ras, selected Ras effectors, or other Ras-related small GTPases. Two-hybrid screens using FLI LRR as bait identified a novel LRR binding partner. The 0.65-kilobase pair (kb) clone from the screen survived additional rounds of stringent two-hybrid pairwise assays, estab...Continue Reading

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