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Yoshida, K. et al.

Yoshida, Suzuki, Honda, Amemiya, Nakatani, Ebina, Narumi, Satoh, Munakata,

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.[1]

References

Leucine-rich repeat region of decorin binds to filamin-A. Yoshida, K., Suzuki, Y., Honda, E., Amemiya, K., Nakatani, T., Ebina, M., Narumi, K., Satoh, K., Munakata, H. Biochimie (2002) [Pubmed]

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