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Fig. 3. Normal targeting of Ykt6 requires both conserved and Ykt6-specific targeting signals in the longin domain. (A) Several distinct longin domains, when removed from their normal protein context, can localize to the Ykt6 vesicular structures. Longin (lgn) domains from Sec22b, VAMP7, Sec22a and sedlin were N-terminally Myc-tagged and expressed in PC12 cells. Subcellular localization of each Myc-longin domain and endogenous rat Ykt6 was examined by double-label fluorescence microscopy using anti-Myc antibody (9E10) and anti-rat-Ykt6 antibody. In each row, the left-hand panel shows the localization of a longin domain of different origin, the middle panel shows endogenous Ykt6 and the right-hand panel is the merged image. Arrows point to punctate structures where the Myc-longin domain and endogenous rat Ykt6 colocalize (22%, 19%, 22% and 14% overlap, respectively). Scale bars, 10 µm. (B) Only the Ykt6 longin domain can direct normal subcellular targeting of the Ykt6 SNARE and prenylation motifs. The longin domain of rat Ykt6 was replaced by exogenous longin domains to create N-terminally Myc-tagged chimeric Ykt6 proteins. Each chimeric rat Ykt6 was expressed in PC12 cells and the subcellular localization was examined by fluorescent microscopy using anti-Myc antibody and FITC-labeled secondary antibody. Scale bars, 10 µm.





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