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A more recent version of this article appeared on February 1, 2002
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Submitted on September 14, 2001
Revised on November 9, 2001
Accepted on November 14, 2001
1 Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242
2 Department of Neurochemistry and Molecular Biology, Leibniz Institute of Neurobiology, Magdeberg, Germany D-39008
* Corresponding author. E-mail address: mark-stamnes{at}uiowa.edu.
Recent studies indicate that regulation of the actin cytoskeleton is important for protein trafficking, but its precise role is unclear. We have characterized the ARF1-dependent assembly of actin on the Golgi apparatus. Actin recruitment involves Cdc42/Rac and requires the activation of the Arp2/3 complex. Although the actin-binding proteins mAbp1 (SH3p7) and drebrin share sequence homology, they are differentially segregated into two distinct ARF-dependent actin complexes. Importantly, the binding of mAbp1, which localizes to the Golgi apparatus, but not drebrin is blocked by occupation of the p23/p24 cargo-protein-binding site on coatomer. Exogenously expressed mAbp1 is mislocalized and inhibits Golgi transport in whole cells. The ability of ARF, vesicle-coat proteins, and cargo to direct the assembly of cytoskeletal structures helps explain how only a handful of vesicle types can mediate the numerous trafficking steps in the cell.
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