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MBC in Press, published online ahead of print June 28, 2006
Mol. Biol. Cell 10.1091/mbc.E05-08-0709

A more recent version of this article appeared on September 1, 2006
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Submitted on August 2, 2005
Revised on June 14, 2006
Accepted on June 15, 2006

Translocation of Endothelial NO Synthase Involves a Ternary Complex with Caveolin-1 and NOSTRIN

Kirstin Schilling,* Nils Opitz,* Anja Wiesenthal, Stefanie Oess, Ritva Tikkanen, Werner Müller-Esterl, and Ann Icking

Institute of Biochemistry II, University of Frankfurt Medical School, D-60590 Frankfurt, Germany

Monitoring Editor: Robert Parton

Recently, we characterized a novel endothelial NO synthase (eNOS) interacting protein, NOSTRIN, which decreases eNOS activity upon overexpression and induces translocation of eNOS away from the plasma membrane. Here, we show that NOSTRIN directly binds to caveolin-1, a well-established inhibitor of eNOS. Because this interaction occurs between the N-terminus of caveolin (positions 1-61) and the central domain of NOSTRIN (positions 323-434), it allows for independent binding of each of the two proteins to eNOS. Consistently, we were able to demonstrate the existence of a ternary complex of NOSTRIN, eNOS, and caveolin-1 in CHO-eNOS cells. In HUVECs, the ternary complex assembles at the plasma membrane upon confluence or thrombin stimulation. In CHO-eNOS cells, NOSTRIN-mediated translocation of eNOS involves caveolin in a process most likely representing caveolar trafficking. Accordingly, trafficking of NOSTRIN/eNOS/caveolin is affected by altering the state of actin filaments or cholesterol levels in the plasma membrane. During caveolar trafficking, NOSTRIN functions as an adaptor to recruit mediators such as dynamin-2 essential for membrane fission. We propose that a ternary complex between NOSTRIN, caveolin-1 and eNOS mediates translocation of endothelial NO synthase, with important implications for the activity and availability of eNOS in the cell.

*These authors contributed equally to this work.

Address correspondence to: Werner Müller-Esterl (wme{at}biochem2.de)




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