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. 2011 May 15;22(10):1677–1685. doi: 10.1091/mbc.E10-08-0677

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© 2011 Capaldo et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 3: — Cyclin D1 forms a PDZ-dependent complex with ZO-3. (A) Western blot of IP experiments with nonimmune (NI) immunoglobulin (Ig)G, cyclin D1, ZO-2, and ZO-3. (B) Immunodepletion assay showing that only a fraction of ZO-3 is bound to cyclin D1 (C) Schematic diagram of ZO-1, ZO-2, and ZO-3 showing multiple PDZ domains within ZO family proteins. (D) Amino acid sequence alignment of human (HS), murine (MM), zebrafish (DR), and Drosophila (Dm) cyclin D1 C-terminal tails showing a conserved class II PDZ binding motif (underlined). (E) GST–ZO-3 fusion proteins interact preferentially with His6–cyclin D1 (H6 CD-1) containing an intact PDZ binding motif and show attenuated binding to His6–cyclin D1 mutant lacking the putative C-terminal PDZ binding motif [H6-CD1(mut)]. (E) Immunodepletion assay showing retention of the majority of cellular ZO-3 in the postbind fractions after iterative cyclin D1 IP.