PRA Isoforms Are Targeted to Distinct Membrane Compartments

The prenylated Rab acceptor (PRA) 1 is a protein that binds prenylated Rab GTPases and inhibits their removal from the membrane by GDI. We describe here the isolation of a second isoform that can also bind Rab GTPases in a guanine nucleotide-independent manner. The two PRA isoforms showed distinct i...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-03, Vol.276 (9), p.6225-6233
Main Authors: Abdul-Ghani, Mohammad, Gougeon, Pierre-Yves, Prosser, Derek C., Da-Silva, Lance F., Ngsee, Johnny K.
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Cell Membrane - chemistry
CHO Cells
Cricetinae
Endoplasmic Reticulum - chemistry
Female
Molecular Sequence Data
Protein Isoforms
Protein Prenylation
rab GTP-Binding Proteins - metabolism
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Summary:The prenylated Rab acceptor (PRA) 1 is a protein that binds prenylated Rab GTPases and inhibits their removal from the membrane by GDI. We describe here the isolation of a second isoform that can also bind Rab GTPases in a guanine nucleotide-independent manner. The two PRA isoforms showed distinct intracellular localization with PRA1 localized primarily to the Golgi complex and PRA2 to the endoplasmic reticulum (ER) compartment. The localization signal was mapped to the COOH-terminal domain of the two proteins. A DXEE motif served to target PRA1 to the Golgi. Mutation of any one of the acidic residues within this motif resulted in significant retention of PRA1 in the ER compartment. Moreover, the introduction of a di-acidic motif to the COOH-terminal domain of PRA2 resulted in partial localization to the Golgi complex. The domain responsible for ER localization of PRA2 was also confined to the carboxyl terminus. Our results showed that these sorting signals were primarily responsible for the differential localization of the two PRA isoforms.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M009073200