Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks

• DOI: 10.1046/j.0960-7412.2002.01252.x
• Publication Date: 2003-03-12T22:06:37Z
• Authors: Claude M. Saint‐Jore; Janet Evins; Henri Batoko; Federica Brandizzi; Ian Moore; Chris Hawes
• Keywords: Brefeldin A; Rab; KDEL

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