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Vol. 15, Issue 8, 3530-3541, August 2004

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The RCP–Rab11 Complex Regulates Endocytic Protein Sorting

Andrew A. Peden ^*, Eric Schonteich , John Chun , Jagath R. Junutula ^*, Richard H. Scheller ^*, and Rytis Prekeris  

^* Genentech, Inc., South San Francisco, California 94080; Department of Cellular and Developmental Biology, School of Medicine, University of Colorado Health Sciences Center, Denver, Colorado 80262

Submitted December 22, 2003; Accepted May 18, 2004
Monitoring Editor: Suzanne Pfeffer

Rab 11 GTPase is an important regulator of endocytic membrane traffic. Recently, we and others have identified a novel family of Rab11 binding proteins, known as Rab11-family interacting proteins (FIPs). One of the family members, Rab coupling protein (RCP), was identified as a protein binding to both Rab4 and Rab11 GTPases. RCP was therefore suggested to serve a dual function as Rab4 and Rab11 binding protein. In this study, we characterized the cellular functions of RCP and mapped its interactions with Rab4 and Rab11. Our data show that RCP interacts only weakly with Rab4 in vitro and does not play the role of coupling Rab11 and Rab4 in vivo. Furthermore, our data indicate that the RCP–Rab11 complex regulates the sorting of transferrin receptors from the degradative to the recycling pathway. We therefore propose that RCP functions primarily as a Rab11 binding protein that regulates protein sorting in tubular endosomes.

Online version of this article contains supporting material. Online version is available at www.molbiolcell.org.

Corresponding author. E-mail address: rytis.prekeris{at}uchsc.edu.

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