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A more recent version of this article appeared on December 1, 2004
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Submitted on May 12, 2004
Revised on August 31, 2004
Accepted on September 1, 2004
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*Faculty of Pharmaceutical Sciences, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan; Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan; and Department of Molecular Infectiology, Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan
Monitoring Editor: Suzanne Pfeffer
Small GTPases of the ADP-ribosylation factor (ARF) family play a key role in membrane trafficking by regulating coated vesicle formation and guanine nucleotide exchange is essential for the ARF function. Brefeldin A blocks the ARF-triggered coat assembly by inhibiting the guanine nucleotide exchange on ARFs and causes disintegration of the Golgi complex and tubulation of endosomal membranes. BIG2 is one of brefeldin A-inhibited guanine nucleotide exchange factors for the ARF GTPases and associated mainly with the trans-Golgi network. In the present study, we have revealed that another population of BIG2 is associated with the recycling endosome and found that expression of a catalytically inactive BIG2 mutant, E738K, selectively induces membrane tubules from this compartment. We have also shown that BIG2 has an exchange activity toward class I ARFs (ARF1 and ARF3) in vivo and inactivation of either ARF exaggerates the BIG2(E738K)-induced tubulation of endosomal membranes. These observations together indicate that BIG2 is implicated in the structural integrity of the recycling endosome through activating class I ARFs.
Research fellow of the 21st Century COE Program.
||Corresponding author.
E-mail: kazunaka{at}pharm.kyoto-u.ac.jp
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