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Originally published In Press as doi:10.1074/jbc.M104831200 on August 8, 2001

J. Biol. Chem., Vol. 276, Issue 42, 39067-39075, October 19, 2001
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Identification and Characterization of a Family of Rab11-interacting Proteins*

Chadwick M. HalesDagger , Richard GrinerDagger , Karen C. Hobdy-Henderson, Matthew C. Dorn, David Hardy, Ravindra Kumar, Jennifer Navarre, Edward K. L. Chan§, Lynne A. Lapierre, and James R. Goldenring

From the Departments of Medicine, Surgery, and Cellular Biology and Anatomy, Institute of Molecular Medicine and Genetics, Medical College of Georgia and the Augusta Veterans Affairs Medical Center, Augusta, Georgia 30912 and § Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037

Rab11a is a small GTP-binding protein enriched in the pericentriolar plasma membrane recycling systems. We hypothesized that Rab11a-binding proteins exist as downstream effectors of its action. Here we define a family of four Rab11-interacting proteins: Rab11-Family Interacting Protein 1 (Rab11-FIP1), Rab11-Family Interacting Protein 2 (Rab11-FIP2), Rab11-Family Interacting Protein 3 (Rab11-FIP3), and pp75/Rip11. All four interacting proteins associated with wild type Rab11a and dominant active Rab11a (Rab11aS20V) as well as Rab11b and Rab25. Rab11-FIP2 also interacted with dominant negative Rab11a (Rab11aS25N) and the tail of myosin Vb. The binding of Rab11-FIP1, Rab11-FIP2, and Rab11-FIP3 to Rab11a was dependent upon a conserved carboxyl-terminal amphipathic alpha -helix. Rab11-FIP1, Rab11-FIP2, and pp75/Rip11 colocalized with Rab11a in plasma membrane recycling systems in both non-polarized HeLa cells and polarized Madin-Darby canine kidney cells. GFP-Rab11-FIP3 also colocalized with Rab11a in HeLa cells. Rab11-FIP1, Rab11-FIP2, and pp75/Rip11 also coenriched with Rab11a and H+K+-ATPase on parietal cell tubulovesicles, and Rab11-FIP1 and Rab11-FIP2 translocated with Rab11a and the H+K+-ATPase upon stimulating parietal cells with histamine. The results suggest that the function of Rab11a in plasma membrane recycling systems is dependent upon a compendium of protein effectors.

* This work was supported by NIDDK Grants DK48370 and DK43405 (to J. R. G.) from the National Institutes of Health, a Veterans Affairs Merit award, and NIAID Grant AI47859 (to E. K. L. C.) from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Both authors contributed equally to this work.

To whom correspondence should be addressed: Institute for Molecular Medicine and Genetics, CB-2803, Medical College of Georgia, 1120 Fifteenth St., Augusta, GA 30912-3175. Tel.: 706-721-8730; Fax: 706-721-7915; E-mail: jgolden@mail.mcg.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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