The POK/AtVPS52 protein localizes to several distinct post-Golgi compartments in sporophytic and gametophytic cells
doi: 10.1093/jxb/ern162
pmid: 18583349
The POK/AtVPS52 protein localizes to several distinct post-Golgi compartments in sporophytic and gametophytic cells
The organization and dynamics of the plant endomembrane system require both universal and plant-specific molecules and compartments. The latter, despite the growing wealth of information, remains poorly understood. From the study of an Arabidopsis thaliana male gametophytic mutant, it was possible to isolate a gene named POKY POLLEN TUBE (POK) essential for pollen tube tip growth. The similarity between the predicted POK protein sequence and yeast Vps52p, a subunit from the GARP/VFT complex which is involved in the docking of vesicles from the prevacuolar compartment to the Golgi apparatus, suggested that the POK protein plays a role in plant membrane trafficking. Genetic analysis of Arabidopsis mutants affecting AtVPS53 or AtVPS54 genes which encode putative POK partners shows a transmission defect through the male gametophyte for all lines, which is similar to the pok mutant. Using a combination of biochemical approaches and specific antiserum it has been demonstrated that the POK protein is present in phylogenetically divergent plant species, associated with membranes and belongs to a high molecular weight complex. Combination of immunolocalization studies and pharmacological approaches in different plant cells revealed that the POK protein associates with Golgi and post-Golgi compartments. The role of POK in post-Golgi endomembrane trafficking and as a member of a putative plant GARP/VFT complex is discussed.
GOLGI AND POST-GOLGI COMPARTMENT, ARABIDOPSIS MUTANT, 570, MESH: Vesicular Transport Proteins, MESH: Microscopy, MESH: Mutation, VESICLE TRAFFICKING, Saccharomyces cerevisiae Proteins, POLLEN TUBE, Arabidopsis, Vesicular Transport Proteins, Golgi Apparatus, BREFELDIN-A, MESH: Arabidopsis Proteins, Flowers, MESH: Golgi Apparatus, MESH: Saccharomyces cerevisiae Proteins, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, MESH: Arabidopsis, [SDV.BV] Life Sciences [q-bio]/Vegetal Biology, RETROMER, 580, COMPLEX, Microscopy, Confocal, Arabidopsis Proteins, POLLEN, ARABIDOPSIS THALIANA, MESH: Immunohistochemistry, PHARMACOLOGIE, Intracellular Membranes, MESH: Multiprotein Complexes, PLANT CELL, MESH: Flowers, Immunohistochemistry, MESH: Intracellular Membranes, HOMOLOG, SNARE, Confocal, Multiprotein Complexes, GARP/VFT COMPLEX, Mutation, GROWTH
GOLGI AND POST-GOLGI COMPARTMENT, ARABIDOPSIS MUTANT, 570, MESH: Vesicular Transport Proteins, MESH: Microscopy, MESH: Mutation, VESICLE TRAFFICKING, Saccharomyces cerevisiae Proteins, POLLEN TUBE, Arabidopsis, Vesicular Transport Proteins, Golgi Apparatus, BREFELDIN-A, MESH: Arabidopsis Proteins, Flowers, MESH: Golgi Apparatus, MESH: Saccharomyces cerevisiae Proteins, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, MESH: Arabidopsis, [SDV.BV] Life Sciences [q-bio]/Vegetal Biology, RETROMER, 580, COMPLEX, Microscopy, Confocal, Arabidopsis Proteins, POLLEN, ARABIDOPSIS THALIANA, MESH: Immunohistochemistry, PHARMACOLOGIE, Intracellular Membranes, MESH: Multiprotein Complexes, PLANT CELL, MESH: Flowers, Immunohistochemistry, MESH: Intracellular Membranes, HOMOLOG, SNARE, Confocal, Multiprotein Complexes, GARP/VFT COMPLEX, Mutation, GROWTH
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