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Vol. 15, Issue 2, 611-624, February 2004

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rabip4' Is an Effector of rab5 and rab4 and Regulates Transport through Early Endosomes

Michael A. Fouraux ^* , Magda Deneka ^* , Viorica Ivan ^* , Annemarie van der Heijden , Jos Raymackers , Denise van Suylekom , Walther J. van Venrooij , Peter van der Sluijs  ^||, and Ger J.M. Pruijn  ^||

Department of Biochemistry, Nijmegen Center for Molecular Life Sciences, University of Nijmegen, Nijmegen, The Netherlands; Department of Cell Biology and Institute of Biomembranes, Utrecht University Medical Center, Utrecht, The Netherlands; and Innogenetics N.V., Zwijnaarde, Ghent, Belgium

Submitted May 29, 2003; Revised October 7, 2003; Accepted October 20, 2003
Monitoring Editor: Vivek Malhotra

We describe the characterization of an 80-kDa protein cross-reacting with a monoclonal antibody against the human La autoantigen. The 80-kDa protein is a variant of rabip4 with an N-terminal extension of 108 amino acids and is expressed in the same cells. For this reason, we named it rabip4'. rabip4' is a peripheral membrane protein, which colocalized with internalized transferrin and EEA1 on early endosomes. Membrane association required the presence of the FYVE domain and was perturbed by the phosphatidylinositol 3-kinase inhibitor wortmannin. Expression of a dominant negative rabip4' mutant reduced internalization and recycling of transferrin from early endosomes, suggesting that it may be functionally linked to rab4 and rab5. In agreement with this, we found that rabip4' colocalized with the two GTPases on early endosomes and bound specifically and simultaneously to the GTP form of both rab4 and rab5. We conclude that rabip4' may coordinate the activities of rab4 and rab5, regulating membrane dynamics in the early endosomal system.

^* These authors contributed equally to this work.

^|| Corresponding author. E-mail address: g.pruijn{at}ncmls.kun.nl or pvander{at}knoware.nl.

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