Molecular Biology of the Cell

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

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

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

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E03-04-0227v1
14/9/3857    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Alory, C.
Right arrow Articles by Balch, W. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Alory, C.
Right arrow Articles by Balch, W. E.

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.




This article has been cited by other articles:


Home page
 GENES CELLSHome page
D. Tanaka, K. Kameyama, H. Okamoto, and M. Doi
Caenorhabditis elegans Rab escort protein (REP-1) differently regulates each Rab protein function and localization in a tissue-dependent manner
Genes Cells, November 1, 2008; 13(11): 1141 - 1157.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Ignatev, S. Kravchenko, A. Rak, R. S. Goody, and O. Pylypenko
A Structural Model of the GDP Dissociation Inhibitor Rab Membrane Extraction Mechanism
J. Biol. Chem., June 27, 2008; 283(26): 18377 - 18384.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
C. Y. Chen and W. E. Balch
The Hsp90 Chaperone Complex Regulates GDI-dependent Rab Recycling
Mol. Biol. Cell, August 1, 2006; 17(8): 3494 - 3507.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
B. H.J. de Graaf, A. Y. Cheung, T. Andreyeva, K. Levasseur, M. Kieliszewski, and H.-m. Wu
Rab11 GTPase-Regulated Membrane Trafficking Is Crucial for Tip-Focused Pollen Tube Growth in Tobacco
PLANT CELL, September 1, 2005; 17(9): 2564 - 2579.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2003 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.