Soluble proteins are transported to the plant vacuole through the secr
etory pathway via membrane-bound vesicles. Targeting of vesicles to ap
propriate organelles requires several membrane-bound and soluble facto
rs that have been characterized in yeast and mammalian systems. For ex
ample, the yeast PEP12 protein is a syntaxin homolog that is involved
in protein transport to the yeast vacuole, Previously, we isolated an
Arabidopsis thaliana homolog of PEP12 by functional complementation of
the yeast pep12 mutant. Antibodies raised against the cytoplasmic por
tion of AtPEP12 have been prepared and used for intracellular localiza
tion of this protein. Biochemical analysis indicates that AtPEP12 does
not localize to the endoplasmic reticulum, Golgi apparatus, plasma me
mbrane, or tonoplast in Arabidopsis plants; furthermore, based on bioc
hemical and electron microscopy immunogold labeling analyses, AtPEP12
is likely to be localized to a post-Golgi compartment in the vacuolar
pathway.