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Originally published as MBC in Press, 10.1091/E03-04-0227 on May 29, 2003

Vol. 14, Issue 9, 3857-3867, September 2003

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Molecular Evolution of the Rab-Escort-Protein/Guanine-Nucleotide-Dissociation-Inhibitor Superfamily

Christelle Alory, and William E. Balch *

Departments of Cell and Molecular Biology and The Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, California 92130

Submitted April 11, 2003; Accepted April 24, 2003
Monitoring Editor: Suzanne Pfeffer

Prenylation of Rab GTPases regulating vesicle traffic by Rab geranylgeranyltransferase (RabGGTase) requires a complex formed by the association of newly synthesized Rab proteins with Rab-escort-protein (REP), the choroideremia-gene-product that is mutated in disease, leading to loss of vision. After delivery to the membrane by the REP–Rab complex, subsequent recycling to the cytosol requires the REP-related guanine-nucleotide-dissociation-inhibitor (GDI). Although REP and GDI share common Rab-binding properties, GDI cannot assist in Rab prenylation and REP cannot retrieve Rab proteins from the membranes. We have now isolated REP mutant proteins that are able to partially function as both REP and GDI. These results provide molecular insight into the functional and evolutionary organization of the REP/GDI superfamily.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03–04–0227. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-04-0227.

* Corresponding author. E-mail address: webalch{at}scripps.edu.




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