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Vol. 14, Issue 7, 2908-2920, July 2003
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* The Henry Wellcome Laboratory of Cell Biology, Division of Biochemistry and
Molecular Biology, Faculty of Biomedical and Life Sciences, University of
Glasgow, Glasgow G12 8QQ. Scotland;
Sinsheimer Laboratories, Department of Molecular, Cellular, and Developmental
Biology, University of California, Santa Cruz, Santa Cruz, California
95064; and
Department of Cellular and Structural Biology School of Medicine, University
of Colorado Health Sciences Center, Denver, Colorado 80262
Submitted March 19, 2003;
Accepted March 23, 2003
Monitoring Editor: Jennifer Lippincott-Schwartz
Arfophilin is an ADP ribosylation factor (Arf) binding protein of unknown function. It is identical to the Rab11 binding protein eferin/Rab11-FIP3, and we show it binds both Arf5 and Rab11. We describe a related protein, arfophilin-2, that interacts with Arf5 in a nucleotide-dependent manner, but not Arf1, 4, or 6 and also binds Rab11. Arfophilin-2 localized to a perinuclear compartment, the centrosomal area, and focal adhesions. The localization of arfophilin-2 to the perinuclear compartment was selectively blocked by overexpression of Arf5-T31N. In contrast, a green fluorescent protein-arfophilin-2 chimera or arfophilin-2 deletions were localized around the centrosome in a region that was also enriched for transferrin receptors and Rab11 but not early endosome markers, suggesting that the distribution of the endosomal recycling compartment was altered. The arfophilins belong to a conserved family that includes Drosophila melanogaster nuclear fallout, a centrosomal protein required for cellularization. Expression of green fluorescent protein-nuclear fallout in HeLa cells resulted in a similar phenotype, indicative of functional homology and thus implicating the arfophilins in mitosis/cytokinesis. We suggest that the novel dual GTPase-binding capacity of the arfophilins could serve as an interface of signals from Rab and Arf GTPases to regulate membrane traffic and integrate distinct signals in the late endosomal recycling compartment.
Present address: Department of Biochemistry and Biophysics, 513 Parnassus
Ave., University of California, San Francisco, San Francisco, CA
94143-0448.
|| Present address: Max Planck Institute for Biochemistry, Department of Cell Biology, Martinsreid, D-82152 Germany.
¶ Corresponding author. E-mail address: g.gould{at}bio.gla.ac.uk.
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