Article
Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1.
Traffic (Copenhagen, Denmark) - 1 May 2005
Szul Tomasz, Garcia-Mata Rafael, Brandon Elizabeth, Shestopal Svetlana, Alvarez Cecilia, Sztul Elizabeth
Abstract excerpt
ADP-ribosylation factor (ARF)-facilitated recruitment of COP I to membranes is required for secretory traffic. The guanine nucleotide exchange factor GBF1 activates ARF and regulates ARF/COP I dynamics at the endoplasmic reticulum (ER)-Golgi interface. Like ARF and coatomer, GBF1 peripherally associates with membranes. ADP-ribosylation factor and coatomer have been shown to rapidly cycle between membranes and...
Topics
- ADP-Ribosylation Factors
- Brefeldin A
- Coat Protein Complex I
- Endoplasmic Reticulum
- Fluorescence Recovery After Photobleaching
- Golgi Apparatus
- Green Fluorescent Proteins
- Guanine Nucleotide Exchange Factors
- HeLa Cells
- Humans
- Models, Biological
- Mutation
- Protein Synthesis Inhibitors