Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

We have fused the signal anchor sequences of a rat sialyl transferase and a human galactosyl transferase along with the Arabidopsis homologue of the yeast HDEL receptor (AtERD2) to the jellyfish green fluorescent protein (GFP) and transiently expressed the chimeric genes in tobacco leaves. All constructs targeted the Golgi apparatus and co-expression with DsRed fusions along with immunolabelling of stably transformed BY2 cells indicated that the fusion proteins located all Golgi stacks. Exposure of tissue to brefeldin A (BFA) resulted in the reversible redistribution of ST-GFP into the endoplasmic reticulum. This effect occurred in the presence of a protein synthesis inhibitor and also in the absence of microtubules or actin filaments. Likewise, reformation of Golgi stacks on removal of BFA was not dependent on either protein synthesis or the cytoskeleton. These data suggest that ER to Golgi transport in the cell types observed does not require cytoskeletal-based mechanochemical motor systems. However, expression of an inhibitory mutant of Arabidopsis Rab 1b (AtRab1b(N121I) significantly slowed down the recovery of Golgi fluorescence in BFA treated cells indicating a role for Rab1 in regulating ER to Golgi anterograde transport.

Type

Journal article

Journal

Plant J

Publication Date

03/2002

Volume

29

Pages

661 - 678

Keywords

Animals, Biological Transport, Brefeldin A, Cell Line, Cells, Cultured, Cycloheximide, Cytoskeleton, Endoplasmic Reticulum, Gene Expression, Golgi Apparatus, Green Fluorescent Proteins, Humans, Luminescent Proteins, Membrane Proteins, Microscopy, Confocal, Plant Epidermis, Plant Leaves, Plants, Genetically Modified, Rats, Recombinant Fusion Proteins, Rhizobium, Tobacco, rab1 GTP-Binding Proteins