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Vol. 14, Issue 2, 361-369, February 2003
*Department of Botany and Plant Sciences and Center for
Plant Cell Biology, University of California, Riverside, California
92521
Plant cells contain several types of vacuoles with specialized
functions. Although the biogenesis of these organelles is well understood at the morphological level, the machinery involved in plant
vacuole formation is largely unknown. We have recently identified an
Arabidopsis mutant, vcl1, that is deficient in
vacuolar formation. VCL1 is homologous to a protein that regulates
membrane fusion at the tonoplast in yeast. On the basis of these
observations, VCL1 is predicted to play a direct role in vacuolar
biogenesis and vesicular trafficking to the vacuole in plants. In this
work, we show that VCL1 forms a complex with AtVPS11 and AtVPS33 in vivo. These two proteins are homologues of proteins that have a
well-characterized role in membrane fusion at the tonoplast in yeast.
VCL1, AtVPS11, and AtVPS33 are membrane-associated and cofractionate
with tonoplast and denser endomembrane markers in subcellular
fractionation experiments. Consistent with this, VCL1, AtVPS11, and
AtVPS33 are found on the tonoplast and the prevacuolar compartment
(PVC) by immunoelectron microscopy. We also show that a VCL1-containing
complex includes SYP2-type syntaxins and is most likely involved in
membrane fusion on both the PVC and tonoplast in vivo. VCL1, AtVPS11,
and AtVPS33 are the first components of the vacuolar biogenesis
machinery to be identified in plants.
Present address: Departamento de Genética Molecular
de Plantas, Centro Nacional de Biotecnología, CSIC, E-28049
Madrid, Spain.
These authors contributed equally to this
work and are listed in alphabetical order.
§
Corresponding author. E-mail address:
nraikhel{at}citrus.ucr.edu.
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