title: Leucine-rich repeat region of decorin binds to filamin-A.
abstract: 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.
authors.affiliation: Department of Biochemistry, Kinki University School of Medicine, Osaka-Sayama, 589-8511, Osaka, Japan. kojiy@med.kindai.ac.jp
authors.forename: Koji
authors.initials: K
authors.lastname: Yoshida
authors.forename: Yasuyuki
authors.initials: Y
authors.lastname: Suzuki
authors.forename: Eiko
authors.initials: E
authors.lastname: Honda
authors.forename: Kana
authors.initials: K
authors.lastname: Amemiya
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Nakatani
authors.forename: Masahito
authors.initials: M
authors.lastname: Ebina
authors.forename: Kou
authors.initials: K
authors.lastname: Narumi
authors.forename: Ken
authors.initials: K
authors.lastname: Satoh
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Munakata
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D015153:Blotting, Western; D002478:Cells, Cultured; D003285:Contractile Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004270:DNA, Circular / Q000235:genetics; D058575:Decorin; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D016326:Extracellular Matrix Proteins; D005347:Fibroblasts / Q000378:metabolism; D064448:Filamins; D005982:Glutathione Transferase / Q000378:metabolism; D006801:Humans; D007930:Leucine / Q000737:chemistry / Q000378:metabolism*; D008168:Lung / Q000166:cytology; D008840:Microfilament Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D011485:Protein Binding; D011509:Proteoglycans / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012091:Repetitive Sequences, Nucleic Acid; D016415:Sequence Alignment; D020798:Two-Hybrid System Techniques
chemical_list: D003285:Contractile Proteins; C546878:DCN protein, human; D004270:DNA, Circular; D058575:Decorin; D016326:Extracellular Matrix Proteins; D064448:Filamins; D008840:Microfilament Proteins; D011509:Proteoglycans; D011993:Recombinant Fusion Proteins; D005982:Glutathione Transferase; D007930:Leucine