An intramolecular t-SNARE complex functions in vivo without the syntaxin NH2-terminal regulatory domain |
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| Authors: | Van Komen Jeffrey S Bai Xiaoyang Scott Brenton L McNew James A |
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| Affiliation: | Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77251, USA. |
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| Abstract: | 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 approximately 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. |
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