Fig. 6

Mapping the part of golgin-245 that captures vesicles. a Schematic diagram of human golgin-245 along with plots for the predicted degree of coiled-coil and disorder along its length. Also shown is the mitochondrial form as in Fig. 1a. b Summary of the vesicle capture activity of the indicated truncations and chimeras of golgin-245. Capture at mitochondria was assayed by immunofluorescent staining of the integral membrane proteins CD-MPR, CI-MPR, TGN46 or Vti1a. A plus sign indicates that capture of all four markers was similar to the wild-type protein, a minus sign indicates that no significant capture was observed. c Alignment of the N-terminus of human golgin-245 with that from the indicated species. Bird, G. gallus; reptile, A. mississippiensis; fish D. rerio; octopus, O. bimaculoides; bee, A. mellifera; fly, D. melanogaster; worm, C. elegans; oyster, C. gigas. d, e Confocal micrographs of HeLa cells expressing the indicated golgin-245 variants and stained for the hemagglutinin tag on the golgin-245 chimera as well as for either TGN46 or CI-MPR (in vesicles captured by golgin-245) as well as for ZFPL1 (a cis-Golgi protein that is not captured). Key constructs from the set shown in (b) are included, with similar results obtained using the vesicle markers CI-MPR, TGN46, CD-MPR, and Vti1a. Scale bars 10 μm