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. 2006 Sep;17(9):3870–3880. doi: 10.1091/mbc.E05-08-0709

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© 2006 by The American Society for Cell Biology

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Figure 3. — NOSTRIN, caveolin-1, and eNOS form a ternary complex. The scaffolding domain of caveolin-1 enhances interaction of NOSTRIN and eNOS. (A) GST pull-down from lysates of CHO-eNOS cells using full-size GST-NOSTRIN and GST-NOSTRIN_1-434, which lacks the eNOS binding SH3 domain. Addition of the Ca²⁺ ionophore A23187 abolishes the interaction of eNOS and caveolin-1. (B) Pull-down from lysates of CHO-eNOS using GST-NOSTRIN. (C) Coimmunoprecipitations from HUVECs using rabbit anti-NOSTRIN or preimmune serum for control. Western blots of immunoprecipitates and lysates were done with mouse anti-eNOS, anti-NOSTRIN, and anti-caveolin-1. The asterisk indicates the position of the immunoglobulin heavy chain. (D) Coimmunoprecipitations from CHO-eNOS cells infected with SFV-HA-NOSTRIN_242-506 using anti-HA. Caveolin-1 peptides cav_82-101 (scaffolding domain), cav_61-81, or unrelated peptide (RLC24) were added to the lysates as indicated. Immunoblots were probed for NOSTRIN (anti-HA) and eNOS.