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. 1998 Jul;9(7):1649–1660. doi: 10.1091/mbc.9.7.1649

Figure 4.

Figure 4

Mitochondrial targeting of VAMP-1B is determined by a combination of a shortened hydrophobic anchor and positive charge at the carboxy terminus. Plasmids encoding VAMP-1 sequences with the FLAG epitope fused to the N terminus were transfected into human endothelial cells, and cells were stained for immunofluorescence with antibodies to either the FLAG epitope (VAMP protein) or Tom20 (mitochondria) after 24 h. In addition to wild type VAMPs 1A and 1B, the constructs included replacement of the carboxy-terminal threonine of VAMP-1A by Arg-Arg-Asp (1A-118RRD), replacement of the carboxy-terminal Arg-Arg-Asp of VAMP-1B by a triple threonine (1B-114TTT), replacement of the carboxy-terminal Asp of VAMP-1B by threonine (1B-116T), and replacement of Arg114 and Arg115 of VAMP-1B by threonines (1B-114TT).