The t-SNARE AtVAM3p resides on the prevacuolar compartment in Arabidopsis root cells.
Protein cargo is trafficked between the organelles of the endomembrane system inside transport vesicles, a process mediated by integral membrane proteins called SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptors) that reside on the surface of the vesicle (v-SNAREs) and target membrane (t-SNAREs). In examining transport of cargo between the trans-Golgi network and the vacuole in Arabidopsis, we have previously characterized AtPEP12p as a t-SNARE residing on the prevacuolar compartment and AtVTI1a as a v-SNARE that interacts with AtPEP12p. Recently, we have begun to characterize AtVAM3p, another Arabidopsis t-SNARE that shows high sequence homology to AtPEP12p. We have found that AtVTI1a also interacts with AtVAM3p, suggesting a role for this t-SNARE in post-Golgi trafficking. AtVAM3p has been suggested to localize to the vacuolar membrane in Arabidopsis cells; however, using specific antisera and expression of epitope-tagged versions of each t-SNARE, we have discovered that AtVAM3p is found on the same prevacuolar structure as AtPEP12p in Arabidopsis root cells.
Sanderfoot
A A
AA
Michigan State University-Department of Energy Plant Research Laboratory, East Lansing, Michigan, 48824-1312, USA.
Kovaleva
V
V
Zheng
H
H
Raikhel
N V
NV
D017360:Arabidopsis / Q000502:physiology* / Q000648:ultrastructure; D029681:Arabidopsis Proteins; D006801:Humans; D007425:Intracellular Membranes / Q000648:ultrastructure; D008565:Membrane Proteins / Q000032:analysis; D010802:Phylogeny; D010940:Plant Proteins / Q000032:analysis* / Q000235:genetics; D018517:Plant Roots / Q000648:ultrastructure; D050765:Qa-SNARE Proteins; D014617:Vacuoles / Q000502:physiology* / Q000648:ultrastructure
D029681:Arabidopsis Proteins; D008565:Membrane Proteins; D010940:Plant Proteins; D050765:Qa-SNARE Proteins; C108430:Vam3 protein, Arabidopsis