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Papers In Press, published online ahead of print March 1, 2009
J. Lipid Res., doi:10.1194/jlr.M800360-JLR200

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Journal of Lipid Research, Vol. 50, 398-404, March 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Differential palmitoylation of the endosomal SNAREs syntaxin 7 and syntaxin 8^*,

Yuhong He and Maurine E. Linder¹

Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110

^* Yuhong He was supported by a postdoctoral fellowship from the American Heart Association (Heartland Affiliate). Work in the authors' laboratory was supported by NIH (GM51466).

The online version of this article (available at http://www.jlr.org) contains supplementary data in the form of one figure.

Published, JLR Papers in Press, October 31, 2008.

¹ To whom correspondence should be addressed. e-mail: mlinder{at}wustl.edu

Palmitoylation is a posttranslational modification that regulates protein trafficking and stability. In this study we investigated whether the endosomal soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins syntaxin 7 and syntaxin 8 are modified with palmitate. Using metabolic labeling and site-directed mutagenesis, we show that human syntaxins 7 and 8 are modified with palmitate through a thioester linkage. Palmitoylation is dependent upon cysteine 239 of human syntaxin 7 and cysteine 214 of syntaxin 8, residues that are located on the cytoplasmic face of the transmembrane domain (TMD). Palmitoylation of syntaxin 8 is minimally affected by the Golgi-disturbing agent brefeldin A (BFA), whereas BFA dramatically inhibits palmitoylation of syntaxin7. The differential effect of BFA suggests that palmitoylation of syntaxins 7 and 8 occurs in distinct subcellular compartments. Palmitoylation does not affect the rate of protein turnover of syntaxins 7 and 8 nor does it influence the steady-state localization of syntaxin 8 in late endosomes. Syntaxin 7 actively cycles between endosomes and the plasma membrane. Palmitoylation-defective syntaxin 7 is selectively retained on the plasma membrane, suggesting that palmitoylation is important for intercompartmental transport of syntaxin 7.

Supplementary key words protein trafficking • fatty acylation • brefeldin A

Abbreviations: BFA, brefeldin A; GFP, green fluorescent protein; SNAP-25, synaptic-associated protein of 25 kDa; SNARE, soluble N-ethylmaleimide-sensitive factor attachment protein receptors; TMD, transmembrane domain

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