Leucine-rich repeat region of decorin binds to filamin-A.

Decorin is a member of the family of small leucine-rich proteoglycans found in the extracellular matrix and has an important role in promoting fiber formation and in controlling cell proliferation. Here, we have investigated whether the leucine-rich repeat (LRR) region of decorin interacts with proteins from human lung fibroblasts by ...
using a yeast two-hybrid assay. We report that the LRR region of decorin interacts with the cytoskeletal protein, filamin-A (ABP-280), a peripheral cytoplasmic protein. This interaction is dependent on the 288 carboxyl-terminal amino acids of filamin-A, which correspond to repeats 22-24 of its conserved beta-sheet structure. We also show that the recombinant LRR region of decorin binds to filamin-A in vitro, and that the deglycosylated core protein of decorin coprecipitates with filamin-A, whereas intact decorin does not. Together, these results suggest that proteins containing the LRR motif that interact with filamin-A may be present in the cytoplasm or at the plasma membrane.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Blotting, Western, Cells, Cultured, Contractile Proteins, DNA, Circular, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Extracellular Matrix Proteins, Fibroblasts, Glutathione Transferase, Humans, Leucine, Lung, Microfilament Proteins, Molecular Sequence Data, Precipitin Tests, Protein Binding, Proteoglycans, Recombinant Fusion Proteins, Repetitive Sequences, Nucleic Acid, Sequence Alignment, Two-Hybrid System Techniques
Biochimie
Date: Apr. 01, 2002
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