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Originally published In Press as doi:10.1074/jbc.M010838200 on March 1, 2001

J. Biol. Chem., Vol. 276, Issue 23, 19820-19827, June 8, 2001
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Syntaxin 7 Complexes with Mouse Vps10p Tail Interactor 1b, Syntaxin 6, Vesicle-associated Membrane Protein (VAMP)8, and VAMP7 in B16 Melanoma Cells*

Nick WadeDagger , Nia J. BryantDagger , Lisa M. Connolly§, Richard J. Simpson§, J. Paul Luzio, Robert C. Piper||, and David E. JamesDagger **

From the Dagger  Institute for Molecular Bioscience and the Department of Physiology and Pharmacology, University of Queensland, St. Lucia, Queensland 4072, the § Joint Protein Structure Laboratory, Ludwig Institute of Cancer Research and the Walter and Eliza Hall Institute, Parkville, Victoria, Australia 3052, the  Welcome Trust Centre for Molecular Mechanisms in Disease, University of Cambridge, Addenbrooke's Hospital, Cambridge CB22XY, United Kingdom, and the || Department of Physiology and Biophysics, University of Iowa, Iowa City, Iowa 52242

Syntaxin 7 is a mammalian target soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) involved in membrane transport between late endosomes and lysosomes. The aim of the present study was to use immunoaffinity techniques to identify proteins that interact with Syntaxin 7. We reasoned that this would be facilitated by the use of cells producing high levels of Syntaxin 7. Screening of a large number of tissues and cell lines revealed that Syntaxin 7 is expressed at very high levels in B16 melanoma cells. Moreover, the expression of Syntaxin 7 increased in these cells as they underwent melanogenesis. From a large scale Syntaxin 7 immunoprecipitation, we have identified six polypeptides using a combination of electrospray mass spectrometry and immunoblotting. These polypeptides corresponded to Syntaxin 7, Syntaxin 6, mouse Vps10p tail interactor 1b (mVti1b), alpha -synaptosome-associated protein (SNAP), vesicle-associated membrane protein (VAMP)8, VAMP7, and the protein phosphatase 1M regulatory subunit. We also observed partial colocalization between Syntaxin 6 and Syntaxin 7, between Syntaxin 6 and mVti1b, but not between Syntaxin 6 and the early endosomal t-SNARE Syntaxin 13. Based on these and data reported previously, we propose that Syntaxin 7/mVti1b/Syntaxin 6 may form discrete SNARE complexes with either VAMP7 or VAMP8 to regulate fusion events within the late endosomal pathway and that these events may play a critical role in melanogenesis.

* This work was supported by the Human Frontiers Science Program (to D. E. J., R. C. P., and J. P. L.), by the Australian Research Council of Australia, and by American Heart Association Grant 9730275N. The Institute for Molecular Bioscience is a special research center of the Australian Research Council.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** National Health and Medical Research Council of Australia principal research fellow. To whom correspondence should be addressed. Tel. and Fax: 61-7-3365-4986; E-mail: D.James@imb.uq.edu.au.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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