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Freeman Jr., T.C., Black, J.L., Bray, H.G., Dagliyan, O., Wu, Y.I., Tripathy, A., Dokholyan, N.V., Leisner, T.M. and Parise, L.V. (2013) Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): Structural and thermodynamic basis of CIB1 promiscuity. Biochemistry, 52, 7082-7090.
http://dx.doi.org/10.1021/bi400678y

has been cited by the following article:

• TITLE: Interaction of calcium- and integrin-binding protein 1 with integrin α11 and its possible involvement in pulmonary fibrosis

  AUTHORS: Koji Yoshida, Ah-Mee Park, Shingen Ozaki, Hiroshi Munakata

  KEYWORDS: Calcium- and Integrin-Binding Protein 1; Fibrosis; Integrin α11; Yeast Two-Hybrid

  JOURNAL NAME: Advances in Biological Chemistry, Vol.4 No.1, February 27, 2014

  ABSTRACT: Integrin α11 (ITGA11) is one of the collagen-binding integrin α chains; however, its biological significance remains unknown. To determine the functions of ITGA11, we performed a yeast two-hybrid screen using the cytoplasmic domain of ITGA11 as bait and transformed an EGY48 yeast strain with the bait-containing plasmid using the plasmid from a human lung fibroblast cDNA library. This screen identified calcium- and integrin-binding protein 1 (CIB1) as prey. Recombinant ITGA11 and CIB1 were expressed in mammalian cells and used in coimmunoprecipitation experiments, which showed that full-length ITGA11 and CIB1 are also associated in vivo. Over-expression of CIB1 in the human lung myofibroblast MRC-5 cells decreased the expression of α-smooth muscle actin and fibronectin. Using a mouse model of pulmonary fibrosis (bleomycin-treatment), we detected elevated expression of CIB1 in lung tissues compared with controls. These data suggest that CIB1 may regulate pulmonary fibrosis in concert with IT-GA11.