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Vol. 10, Issue 7, 2251-2264, July 1999
§ and
*Department of Energy-Plant Research Laboratory, Michigan
State University, East Lansing, Michigan 48824; and
Membrane traffic in eukaryotic cells relies on recognition between
v-SNAREs on transport vesicles and t-SNAREs on target membranes. Here
we report the identification of AtVTI1a and AtVTI1b, two Arabidopsis homologues of the yeast v-SNARE Vti1p, which
is required for multiple transport steps in yeast. AtVTI1a and AtVTI1b
share 60% amino acid identity with one another and are 32 and 30%
identical to the yeast protein, respectively. By suppressing defects
found in specific strains of yeast vti1
temperature-sensitive mutants, we show that AtVTI1a can substitute for
Vti1p in Golgi-to-prevacuolar compartment (PVC) transport, whereas
AtVTI1b substitutes in two alternative pathways: the vacuolar import of
alkaline phosphatase and the so-called cytosol-to-vacuole pathway used
by aminopeptidase I. Both AtVTI1a and AtVTI1b are
expressed in all major organs of Arabidopsis. Using
subcellular fractionation and immunoelectron microscopy, we show that
AtVTI1a colocalizes with the putative vacuolar cargo receptor AtELP on
the trans-Golgi network and the PVC. AtVTI1a also
colocalizes with the t-SNARE AtPEP12p to the PVC. In addition, AtVTI1a
and AtPEP12p can be coimmunoprecipitated from plant cell extracts. We
propose that AtVTI1a functions as a v-SNARE responsible for targeting
AtELP-containing vesicles from the trans-Golgi
network to the PVC, and that AtVTI1b is involved in a different
membrane transport process.
Institute of Molecular Biology, University of Oregon,
Eugene, Oregon 97403-1229
These authors contributed equally to this work.
Corresponding author. E-mail address:
nraikhel{at}pilot.msu.edu.
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