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Originally published In Press as doi:10.1074/jbc.M209760200 on October 11, 2002

J. Biol. Chem., Vol. 277, Issue 51, 49352-49359, December 20, 2002
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Erf4p and Erf2p Form an Endoplasmic Reticulum-associated Complex Involved in the Plasma Membrane Localization of Yeast Ras Proteins*

Lihong ZhaoDagger , Sandra Lobo§, Xiangwen Dong§, Addison D. Ault§, and Robert J. DeschenesDagger §

From the Dagger  Genetics Program and § Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242

Ras oncogene proteins are plasma membrane-associated signal transducers that are found in all eukaryotes. Posttranslational addition of lipid to a carboxyl-terminal CaaX box (where "C" represents a cysteine, "a" is generally an aliphatic residue, and X can be any amino acid) is required to target Ras proteins to the cytosolic surface of the plasma membrane. The pathway by which Ras translocates from the endoplasmic reticulum to the plasma membrane is currently not clear. We have performed a genetic screen to identify components of the Ras plasma membrane localization pathway. Mutations in two genes, ERF2 and ERF4/SHR5, have been shown to affect the palmitoylation and subcellular localization of Ras proteins. In this report, we show that Erf4p is localized on the endoplasmic reticulum as a peripheral membrane protein in a complex with Erf2p, an integral membrane protein that was identified from the same genetic screen. Erf2p has been shown to be required for the plasma membrane localization of GFP-Ras2p via a pathway distinct from the classical secretory pathway (X. Dong and R. J. Deschenes, manuscript in preparation). We show here that Erf4p, like Erf2p, is involved in the plasma membrane localization of Ras2p. Erf2p and Erf4p represent components of a previously uncharacterized subcellular transport pathway involved in the plasma membrane targeting of Ras proteins.

* This work was supported by NCI, National Institutes of Health, Grant CA50211 (to R. J. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Biochemistry, 3135 MERF, University of Iowa, Iowa City, Iowa 52242. Tel.: 319-335-7884; Fax: 319-384-4770; E-mail: robert-deschenes@uiowa.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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