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A more recent version of this article appeared on May 1, 2003
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Submitted on November 4, 2002
Revised on January 1, 2003
Accepted on January 13, 2003
1 Department of Molecular Medicine, Cornell University, Ithaca NY 14853-6401
2 Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6058
* Corresponding author. E-mail address: rnc8{at}cornell.edu.
The vast majority Rab proteins are post-translationally modified with two geranylgeranyl lipid moieties that enable their stable association with membranes. In this study, we present evidence to demonstrate that there is a specific lipid requirement for Rab protein localization and function. Substitution of different prenyl anchors on Rab GTPases does not lead to correct function. In the case of YPT1 and SEC4, two essential Rab genes in S. cerevisiae, alternative lipid tails cannot support life when present as the sole source of YPT1 and SEC4. Furthermore, our data suggest that double geranyl-geranyl groups are required for Rab proteins to correctly localize to their characteristic organelle membrane. We have identified a factor, Yip1p that specifically binds the digeranylgeranylated Rab and does not interact with mono-prenylated Rab proteins. This is the first demonstration that the double prenylation modification of Rab proteins is an important feature in the function of this small GTPase family, and adds specific prenylation to the already known determinants of Rab localization.
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