Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein.

Authors: Andres, DA  Seabra, MC  Brown, MS  Armstrong, SA  Smeland, TE  Cremers, FP  Goldstein, JL 
Citation: Andres DA, etal., Cell 1993 Jun 18;73(6):1091-9.
Pubmed: (View Article at PubMed) PMID:8513495

cDNA cloning of component A of rat Rab geranylgeranyl transferase confirms identity of the protein with the human choroideremia gene product and its resemblance to Rab3A guanine nucleotide dissociation inhibitor (GDI), which binds prenylated Rabs. In biochemical assays we demonstrate that component A binds unprenylated Rab1A, presents it to the catalytic component B, and remains bound to it after the geranylgeranyl transfer reaction. In the absence of detergents, the reaction terminates when all of component A is occupied with prenylated Rab. Detergents allow multiple rounds of catalysis, apparently by dissociating the component A-Rab complex and thus allowing recycling of component A. Within the cell, component A may be regenerated by transferring its prenylated Rab to a protein acceptor, such as Rab3A GDI. In view of its function in escorting Rab proteins during and presumably after the prenyl transfer reaction, we propose to rename component A as Rab escort protein (REP). A genetic defect in REP underlies human choroideremia, a disease of retinal degeneration.


Gene Ontology Annotations
Objects Annotated
Objects referenced in this article

Additional Information

CRRD Object Information
CRRD ID: 704419
Created: 2003-09-18
Species: All species
Last Modified: 2003-09-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.