Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 15 January 1993:
Vol. 259. no. 5093, pp. 377 - 381
DOI: 10.1126/science.8380507
Prev | Table of Contents | Next

Articles

Science, Vol 259, Issue 5093, 377-381
Copyright © 1993 by American Association for the Advancement of Science

articles

Retinal degeneration in choroideremia: deficiency of rab geranylgeranyl transferase

MC Seabra, MS Brown, and JL Goldstein

Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.

Rab geranylgeranyl transferase (GG transferase) is a two-component enzyme that attaches 20-carbon isoprenoid groups to cysteine residues in Rab proteins, a family of guanosine triphosphate-binding proteins that regulate vesicular traffic. The mutant gene in human choroideremia, an X-linked form of retinal degeneration, encodes a protein that resembles component A of rat Rab GG transferase. Lymphoblasts from choroideremia subjects showed a marked deficiency in the activity of component A, but not component B, of Rab GG transferase. The deficiency was more pronounced when the substrate was Rab3A, a synaptic vesicle protein, than it was when the substrate was Rab1A, a protein of the endoplasmic reticulum. The data imply the existence of multiple component A proteins, one of which is missing in choroideremia.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A Rab escort protein integrates the secretion system with TOR signaling and ribosome biogenesis.
J. Singh and M. Tyers (2009)
Genes & Dev. 23, 1944-1958
   Abstract »    Full Text »    PDF »
Single choroideremia Gene in Nonmammalian Vertebrates Explains Early Embryonic Lethality of the Zebrafish Model of Choroideremia.
M. Moosajee, M. Tulloch, R. A. Baron, C. Y. Gregory-Evans, J. B. Pereira-Leal, and M. C. Seabra (2009)
Invest. Ophthalmol. Vis. Sci. 50, 3009-3016
   Abstract »    Full Text »    PDF »
Syndromic Choroideremia: Sublocalization of Phenotypes Associated with Martin-Probst Deafness Mental Retardation Syndrome.
C. M. Poloschek, B. Kloeckener-Gruissem, L. L. Hansen, M. Bach, and W. Berger (2008)
Invest. Ophthalmol. Vis. Sci. 49, 4096-4104
   Abstract »    Full Text »    PDF »
New Type of Mutations in Three Spanish Families with Choroideremia.
M. Garcia-Hoyos, I. Lorda-Sanchez, P. Gomez-Garre, C. Villaverde, D. Cantalapiedra, A. Bustamante, D. Diego-Alvarez, E. Vallespin, J. Gallego-Merlo, M. J. Trujillo, et al. (2008)
Invest. Ophthalmol. Vis. Sci. 49, 1315-1321
   Abstract »    Full Text »    PDF »
When intracellular logistics fails - genetic defects in membrane trafficking.
V. M. Olkkonen and E. Ikonen (2006)
J. Cell Sci. 119, 5031-5045
   Abstract »    Full Text »    PDF »
Multiple Factors Contribute to Inefficient Prenylation of Rab27a in Rab Prenylation Diseases.
B. Larijani, A. N. Hume, A. K. Tarafder, and M. C. Seabra (2003)
J. Biol. Chem. 278, 46798-46804
   Abstract »    Full Text »    PDF »
Molecular Evolution of the Rab-Escort-Protein/Guanine-Nucleotide-Dissociation-Inhibitor Superfamily.
C. Alory and W. E. Balch (2003)
Mol. Biol. Cell 14, 3857-3867
   Abstract »    Full Text »    PDF »
Organization of the Human IMPG2 Gene and Its Evaluation as a Candidate Gene in Age-Related Macular Degeneration and Other Retinal Degenerative Disorders.
M. H. Kuehn, E. M. Stone, and G. S. Hageman (2001)
Invest. Ophthalmol. Vis. Sci. 42, 3123-3129
   Abstract »    Full Text »    PDF »
Efficient Prenylation by a Plant Geranylgeranyltransferase-I Requires a Functional CaaL Box Motif and a Proximal Polybasic Domain.
D. Caldelari, H. Sternberg, M. Rodriguez-Concepcion, W. Gruissem, and S. Yalovsky (2001)
Plant Physiology 126, 1416-1429
   Abstract »    Full Text »    PDF »
Rab27a: A Key to Melanosome Transport in Human Melanocytes.
P. Bahadoran, E. Aberdam, F. Mantoux, R. Busca, K. Bille, N. Yalman, G. de Saint-Basile, R. Casaroli-Marano, J.-P. Ortonne, and R. Ballotti (2001)
J. Cell Biol. 152, 843-850
   Abstract »    Full Text »    PDF »
Rab27a Regulates the Peripheral Distribution of Melanosomes in Melanocytes.
A. N. Hume, L. M. Collinson, A. Rapak, A. Q. Gomes, C. R. Hopkins, and M. C. Seabra (2001)
J. Cell Biol. 152, 795-808
   Abstract »    Full Text »    PDF »
Genetic Defects of Intracellular-Membrane Transport.
V. M. Olkkonen and E. Ikonen (2000)
N. Engl. J. Med. 343, 1095-1104
   Full Text »    PDF »
Molecular Basis for Rab Prenylation.
C. Alory and W. E. Balch (2000)
J. Cell Biol. 150, 89-104
   Abstract »    Full Text »    PDF »
Heterogeneous gene expression from the inactive X chromosome: An X-linked gene that escapes X inactivation in some human cell lines but is inactivated in others.
L. Carrel and H. F. Willard (1999)
PNAS 96, 7364-7369
   Abstract »    Full Text »    PDF »
The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase.
M. Linari, M. Ueffing, F. Manson, A. Wright, T. Meitinger, and J. Becker (1999)
PNAS 96, 1315-1320
   Abstract »    Full Text »    PDF »
HMG-CoA Reductase Inhibitors Reduce MMP-9 Secretion by Macrophages.
S. Bellosta, D. Via, M. Canavesi, P. Pfister, R. Fumagalli, R. Paoletti, and F. Bernini (1998)
Arterioscler Thromb Vasc Biol 18, 1671-1678
   Abstract »    Full Text »    PDF »
Single prenyl-binding site on protein prenyl transferases.
L. Desnoyers and M. C. Seabra (1998)
PNAS 95, 12266-12270
   Abstract »    Full Text »    PDF »
Biochemical Characterization and Subcellular Localization of the Mouse Retinitis Pigmentosa GTPase Regulator (mRpgr).
D. Yan, P. K. Swain, D. Breuer, R. M. Tucker, W. Wu, R. Fujita, A. Rehemtulla, D. Burke, and A. Swaroop (1998)
J. Biol. Chem. 273, 19656-19663
   Abstract »    Full Text »    PDF »
The Yeast Rab Escort Protein Binds Intracellular Membranes in Vivo and in Vitro.
M. Miaczynska, S. Lorenzetti, U. Bialek, R. M. Benito-Moreno, R. J. Schweyen, and A. Ragnini (1997)
J. Biol. Chem. 272, 16972-16977
   Abstract »    Full Text »    PDF »
In situ inhibition of vesicle transport and protein processing in the dominant negative Rab1 mutant of Drosophila.
A Satoh, F Tokunaga, S Kawamura, and K Ozaki (1997)
J. Cell Sci. 110, 2943-2953
   Abstract »    PDF »
Rin, a Neuron-Specific and Calmodulin-Binding Small G-Protein, and Rit Define a Novel Subfamily of Ras Proteins.
C.-H. J. Lee, N. G. Della, C. E. Chew, and D. J. Zack (1996)
J. Neurosci. 16, 6784-6794
   Abstract »    Full Text »    PDF »
Nucleotide Dependence of Rab Geranylgeranylation. Rab ESCORT PROTEIN INTERACTS PREFERENTIALLY WITH GDP-BOUND Rab.
M. C. Seabra and M. C. Seabra (1996)
J. Biol. Chem. 271, 14398-14404
   Abstract »    Full Text »    PDF »
Protein Prenyltransferases.
P. J. Casey and M. C. Seabra (1996)
J. Biol. Chem. 271, 5289-5292
   Full Text »    PDF »
Biosynthesis of the Unsaturated 14-Carbon Fatty Acids Found on the N Termini of Photoreceptor-specific Proteins.
J. C. DeMar Jr., T. G. Wensel, and R. E. Anderson (1996)
J. Biol. Chem. 271, 5007-5016
   Abstract »    Full Text »    PDF »
Mechanism of Digeranylgeranylation of Rab Proteins.
F. Shen and M. C. Seabra (1996)
J. Biol. Chem. 271, 3692-3698
   Abstract »    Full Text »    PDF »
Cytoplasmic Domain of Rhodopsin Is Essential for Post-Golgi Vesicle Formation in a Retinal Cell-free System.
D. Deretic, B. Puleo-Scheppke, and C. Trippe (1996)
J. Biol. Chem. 271, 2279-2286
   Abstract »    Full Text »    PDF »
Deficient Geranylgeranylation of Ram/Rab27 in Choroideremia.
M. C. Seabra, Y. K. Ho, and J. S. Anant (1995)
J. Biol. Chem. 270, 24420-24427
   Abstract »    Full Text »    PDF »
Protein lipidation in cell signaling.
P. Casey (1995)
Science 268, 221-225
   Abstract »    PDF »
CAAX Geranylgeranyl Transferase Transfers Farnesyl as Efficiently as Geranylgeranyl to RhoB.
S. A. Armstrong, V. C. Hannah, J. L. Goldstein, and M. S. Brown (1995)
J. Biol. Chem. 270, 7864-7868
   Abstract »    Full Text »    PDF »
Polylysine and CVIM Sequences of K-RasB Dictate Specificity of Prenylation and Confer Resistance to Benzodiazepine Peptidomimetic in Vitro.
G. L. James, J. L. Goldstein, and M. S. Brown (1995)
J. Biol. Chem. 270, 6221-6226
   Abstract »    Full Text »    PDF »
The GDP/GTP Cycle of Rab5 in the Regulation of Endocytotic Membrane Traffic.
G. Vitale, K. Alexandrov, O. Ullrich, H. Horuichi, A. Giner, C. Dobson, O. Baykova, H. Gournier, H. Stenmark, and M. Zerial (1995)
Cold Spring Harb Symp Quant Biol 60, 211-220
   Abstract »    PDF »
rab8 in retinal photoreceptors may participate in rhodopsin transport and in rod outer segment disk morphogenesis.
D Deretic, L. Huber, N Ransom, M Mancini, K Simons, and D. Papermaster (1995)
J. Cell Sci. 108, 215-224
   Abstract »    PDF »
Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells.
G. James, J. Goldstein, M. Brown, T. Rawson, T. Somers, R. McDowell, C. Crowley, B. Lucas, A. Levinson, and J. Marsters Jr (1993)
Science 260, 1937-1942
   Abstract »    PDF »
Protein prenylation: a mediator of protein-protein interactions.
C. Marshall (1993)
Science 259, 1865-1866
   PDF »
Rab6 is associated with a compartment that transports rhodopsin from the trans-Golgi to the site of rod outer segment disk formation in frog retinal photoreceptors.
D Deretic and D. Papermaster (1993)
J. Cell Sci. 106, 803-813
   Abstract »    PDF »
Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis.
J. C. Detter, Q. Zhang, E. H. Mules, E. K. Novak, V. S. Mishra, W. Li, E. B. McMurtrie, V. T. Tchernev, M. R. Wallace, M. C. Seabra, et al. (2000)
PNAS 97, 4144-4149
   Abstract »    Full Text »    PDF »
Increased Myocardial Rab GTPase Expression: A Consequence and Cause of Cardiomyopathy.
G. Wu, M. G. Yussman, T. J. Barrett, H. S. Hahn, H. Osinska, G. M. Hilliard, X. Wang, T. Toyokawa, A. Yatani, R. A. Lynch, et al. (2001)
Circ. Res. 89, 1130-1137
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)