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A more recent version of this article appeared on February 1, 2004
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Submitted on May 29, 2003
Revised on October 7, 2003
Accepted on October 20, 2003
1 Department of Biochemistry, Nijmegen Center for Molecular Life Sciences, University of Nijmegen, Nijmegen, The Netherlands, Contributed equally to this work
2 Department of Cell Biology and Institute of Biomembranes, Utrecht University Medical Center, Utrecht, The Netherlands, Contributed equally to this work
3 Department of Biochemistry, Nijmegen Center for Molecular Life Sciences, University of Nijmegen, Nijmegen, The Netherlands
4 Innogenetics N.V., Zwijnaarde, Ghent, Belgium
5 Department of Cell Biology and Institute of Biomembranes, Utrecht University Medical Center, Utrecht, The Netherlands
* Corresponding author. E-mail address: G.Pruijn{at}ncmls.kun.nl.
We describe the characterization of an 80 kDa protein cross-reacting with a monoclonal antibody (mAb) 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 PI3-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.
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