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. 2010 Mar 29;285(22):17156–17165. doi: 10.1074/jbc.M109.080523

FIGURE 4.

FIGURE 4.

Location of FLNa-binding site of CFTR. A, amino acid sequence alignment of the CFTR1–25 (human) and FLNa-binding sites of human glycoprotein Ibα (GPIbα), β integrins, FilGAP, and migfilin. Amino acids indicated with asterisks face a glove generated between the C and D strands of the IgFLNa domain which are mainly involved in binding interaction. Solid and dotted underlines indicate residues 1–17 and 8–25 of CFTR peptides used for binding assay in C. Red and blue amino acids indicate residues mutated in CF patients (P5L, S13F, L15P, and W19C). B, comparison of the amino acid sequence similarity predicted from the full-length nucleotide sequences of the CFTR of monkey (UniProt accession number, Q7JII7), bovine (P35071), sheep (Q00555), horse (Q2QLA3), pig (Q6PQZ2), dog (Q5U820), rabbit (Q00554), rat (P34158), mouse (P26361), and chicken (A0M8U4). Amino acids indicated with asterisks are mainly involved in binding interaction. Residues differ from human CFTR (green). C, CFTR peptide pulldown assay with purified FLNa. Bound FLNa was detected by immunoblotting (IB) with anti-FLNa mAb.