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A more recent version of this article appeared on February 1, 2003
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Submitted on August 15, 2002
Revised on October 4, 2002
Accepted on October 31, 2002
1 Department of Botany and Plant Sciences and Center for Plant Cell Biology, 2109 Batchelor Hall, University of California, Riverside, CA 92521, USA (present address: Departamento de Genética Molecular de Plantas, Centro Nacional de Biotecnología, CSIC, E-28049 Madrid, Spain)
2 Department of Botany and Plant Sciences and Center for Plant Cell Biology, 2109 Batchelor Hall, University of California, Riverside, CA 92521, USA
* Corresponding author. E-mail address: nraikhel{at}citrus.ucr.edu.
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. Based on 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 co-fractionate 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 likely involved in membrane fusion on both PVC and tonoplast in vivo. VCL1, AtVPS11, and AtVPS33 are the first components of the vacuolar biogenesis machinery identified in plants.
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