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J Biol Chem, Vol. 273, Issue 14, 7920-7927, April 3, 1998
From the Department of Physiology and the Cell Regulation Graduate
Program, University of Texas Southwestern Medical Center,
Dallas, Texas 75235
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
Identification of the Binding Partners for Flightless I, A Novel
Protein Bridging the Leucine-rich Repeat and the Gelsolin
Superfamilies
-
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, establishing a specific interaction. Binding to FLI LRR was corroborated by
co-immunoprecipitation with FLI LRR. The translated sequence of the FLI
LRR associated protein (FLAP) encodes a novel protein not represented
in the data base. Northern blot analyses revealed four FLAP messages of
approximately 2.7, 2.9, 3.3, and 5.1 kb, which are differentially expressed in the tissues tested. Skeletal and cardiac muscles are
particularly rich in the 3.3-kb FLAP message, and the FLI message as
well. Full-length FLAP clones were isolated from a mouse skeletal
muscle cDNA library. They have an open reading frame which encodes
for a protein containing 626 amino acids. Sequence analyses predict
that the FLAP protein is rich in -helices and contains stretches of
dimeric coiled coil in its middle region and COOH terminus. The
identification of actin and FLAP as the binding ligands for the
gelsolin-like domain and the LRR domain, respectively, suggests that
FLI may link the actin cytoskeleton to other modules implicated in
intermolecular recognition and structural organization.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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