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Published online 9 January 2006. doi:10.1083/jcb.200507138
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 2, 295-307
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Article

An intramolecular t-SNARE complex functions in vivo without the syntaxin NH2-terminal regulatory domain



Jeffrey S. Van Komen, Xiaoyang Bai, Brenton L. Scott, and James A. McNew

Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77251

Correspondence to James A. McNew: mcnew{at}rice.edu

Membrane fusion in the secretory pathway is mediated by SNAREs (located on the vesicle membrane [v-SNARE] and the target membrane [t-SNARE]). In all cases examined, t-SNARE function is provided as a three-helix bundle complex containing three ~70–amino acid SNARE motifs. One SNARE motif is provided by a syntaxin family member (the t-SNARE heavy chain), and the other two helices are contributed by additional t-SNARE light chains. The syntaxin family is the most conformationally dynamic group of SNAREs and appears to be the major focus of SNARE regulation. An NH2-terminal region of plasma membrane syntaxins has been assigned as a negative regulatory element in vitro. This region is absolutely required for syntaxin function in vivo. We now show that the required function of the NH2-terminal regulatory domain (NRD) of the yeast plasma membrane syntaxin, Sso1p, can be circumvented when t-SNARE complex formation is made intramolecular. Our results suggest that the NRD is required for efficient t-SNARE complex formation and does not recruit necessary scaffolding factors.

Abbreviations used in this paper: IHR, interhelical region; NRD, NH2-terminal regulatory domain; 5-FOA, 5-fluoorotic acid.


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