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A more recent version of this article appeared on July 1, 2003
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Submitted on March 19, 2003
Accepted on March 24, 2003
1 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 (present address: Department of Biochemistry and Biophysics, University of California, San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143-0448, USA)
2 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
3 Sinsheimer Laboratories, Department of Molecular, Cellular and Developmental Biology, University of California, Santa Cruz, CA 95064, USA
4 Department of Cellular and Structural Biology School of Medicine, University of Colorado Health Sciences Center 4200 E. Ninth Ave., Room 4520, B111 Denver, CO 80262, USA
5 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 (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.
Arfophilin is an ADP ribosylation factor 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 fashion, but not Arf1, 4 or 6 and also binds Rab11. Arfophilin-2 localised to a peri-nuclear compartment, the centrosomal area and focal adhesions. The localisation of arfophilin-2 to the peri-nuclear compartment was selectively blocked by over-expression of Arf5-T31N. By contrast, a GFP-arfophilin-2 chimera or arfophilin-2 deletions were localised 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 D. melanogaster nuclear fallout, a centrosomal protein required for cellularization. Expression of GFP-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.
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